Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains.
Liquids transforming into solids by the removal of heat.
The technique of using a cryostat or freezing microtome, in which the temperature is regulated to -20 degrees Celsius, to cut ultrathin frozen sections for microscopic (usually, electron microscopic) examination.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A genus of ADENOVIRIDAE that comprises viruses of several species of MAMMALS and BIRDS. The type species is Ovine adenovirus D.
The technique of washing tissue specimens with a concentrated solution of a heavy metal salt and letting it dry. The specimen will be covered with a very thin layer of the metal salt, being excluded in areas where an adsorbed macromolecule is present. The macromolecules allow electrons from the beam of an electron microscope to pass much more readily than the heavy metal; thus, a reversed or negative image of the molecule is created.
The outer protein protective shell of a virus, which protects the viral nucleic acid.
A technique of inputting two-dimensional images into a computer and then enhancing or analyzing the imagery into a form that is more useful to the human observer.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
Proteins that form the CAPSID of VIRUSES.
A tomographic technique for obtaining 3-dimensional images with transmission electron microscopy.
A form of arboviral encephalitis (which primarily affects horses) endemic to western and central regions of NORTH AMERICA. The causative organism (ENCEPHALOMYELITIS VIRUS, WESTERN EQUINE) may be transferred to humans via the bite of mosquitoes (CULEX tarsalis and others). Clinical manifestations include headache and influenza-like symptoms followed by alterations in mentation, SEIZURES, and COMA. DEATH occurs in a minority of cases. Survivors may recover fully or be left with residual neurologic dysfunction, including PARKINSONISM, POSTENCEPHALITIC. (From Joynt, Clinical Neurology, 1996, Ch26, pp8-9)
The infective system of a virus, composed of the viral genome, a protein core, and a protein coat called a capsid, which may be naked or enclosed in a lipoprotein envelope called the peplos.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Imaging methods that result in sharp images of objects located on a chosen plane and blurred images located above or below the plane.
The assembly of VIRAL STRUCTURAL PROTEINS and nucleic acid (VIRAL DNA or VIRAL RNA) to form a VIRUS PARTICLE.
The use of instrumentation and techniques for visualizing material and details that cannot be seen by the unaided eye. It is usually done by enlarging images, transmitted by light or electron beams, with optical or magnetic lenses that magnify the entire image field. With scanning microscopy, images are generated by collecting output from the specimen in a point-by-point fashion, on a magnified scale, as it is scanned by a narrow beam of light or electrons, a laser, a conductive probe, or a topographical probe.
A genus of PICORNAVIRIDAE inhabiting primarily the respiratory tract of mammalian hosts. It includes over 100 human serotypes associated with the COMMON COLD.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The process of generating three-dimensional images by electronic, photographic, or other methods. For example, three-dimensional images can be generated by assembling multiple tomographic images with the aid of a computer, while photographic 3-D images (HOLOGRAPHY) can be made by exposing film to the interference pattern created when two laser light sources shine on an object.
The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Preservation of cells, tissues, organs, or embryos by freezing. In histological preparations, cryopreservation or cryofixation is used to maintain the existing form, structure, and chemical composition of all the constituent elements of the specimens.
Univalent antigen-binding fragments composed of one entire IMMUNOGLOBULIN LIGHT CHAIN and the amino terminal end of one of the IMMUNOGLOBULIN HEAVY CHAINS from the hinge region, linked to each other by disulfide bonds. Fab contains the IMMUNOGLOBULIN VARIABLE REGIONS, which are part of the antigen-binding site, and the first IMMUNOGLOBULIN CONSTANT REGIONS. This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The characteristic three-dimensional shape of a molecule.
Microscopy in which the object is examined directly by an electron beam scanning the specimen point-by-point. The image is constructed by detecting the products of specimen interactions that are projected above the plane of the sample, such as backscattered electrons. Although SCANNING TRANSMISSION ELECTRON MICROSCOPY also scans the specimen point by point with the electron beam, the image is constructed by detecting the electrons, or their interaction products that are transmitted through the sample plane, so that is a form of TRANSMISSION ELECTRON MICROSCOPY.
The physical characteristics and processes of biological systems.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The study of PHYSICAL PHENOMENA and PHYSICAL PROCESSES as applied to living things.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
A type of endoplasmic reticulum (ER) where polyribosomes are present on the cytoplasmic surfaces of the ER membranes. This form of ER is prominent in cells specialized for protein secretion and its principal function is to segregate proteins destined for export or intracellular utilization.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample.
Proteins prepared by recombinant DNA technology.
Established cell cultures that have the potential to propagate indefinitely.
Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.
Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.
The type species of ALPHAVIRUS normally transmitted to birds by CULEX mosquitoes in Egypt, South Africa, India, Malaya, the Philippines, and Australia. It may be associated with fever in humans. Serotypes (differing by less than 17% in nucleotide sequence) include Babanki, Kyzylagach, and Ockelbo viruses.

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. (1/1790)

Amyloid fibrils are assemblies of misfolded proteins and are associated with pathological conditions such as Alzheimer's disease and the spongiform encephalopathies. In the amyloid diseases, a diverse group of normally soluble proteins self-assemble to form insoluble fibrils. X-ray fibre diffraction studies have shown that the protofilament cores of fibrils formed from the various proteins all contain a cross-beta-scaffold, with beta-strands perpendicular and beta-sheets parallel to the fibre axis. We have determined the threedimensional structure of an amyloid fibril, formed by the SH3 domain of phosphatidylinositol-3'-kinase, using cryo-electron microscopy and image processing at 25 A resolution. The structure is a double helix of two protofilament pairs wound around a hollow core, with a helical crossover repeat of approximately 600 A and an axial subunit repeat of approximately 27 A. The native SH3 domain is too compact to fit into the fibril density, and must unfold to adopt a longer, thinner shape in the amyloid form. The 20x40-A protofilaments can only accommodate one pair of flat beta-sheets stacked against each other, with very little inter-strand twist. We propose a model for the polypeptide packing as a basis for understanding the structure of amyloid fibrils in general.  (+info)

MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. (2/1790)

Terminal cell differentiation is correlated with the extensive sequestering of previously active genes into compact transcriptionally inert heterochromatin. In vertebrate blood cells, these changes can be traced to the accumulation of a developmentally regulated heterochromatin protein, MENT. Cryoelectron microscopy of chicken granulocyte chromatin, which is highly enriched with MENT, reveals exceptionally compact polynucleosomes, which maintain a level of higher order folding above that imposed by linker histones. The amino acid sequence of MENT reveals a close structural relationship with serpins, a large family of proteins known for their ability to undergo dramatic conformational transitions. Conservation of the "hinge region" consensus in MENT indicates that this ability is retained by the protein. MENT is distinguished from the other serpins by being a basic protein, containing several positively charged surface clusters, which are likely to be involved in ionic interactions with DNA. One of the positively charged domains bears a significant similarity to the chromatin binding region of nuclear lamina proteins and with the A.T-rich DNA-binding motif, which may account for the targeting of MENT to peripheral heterochromatin. MENT ectopically expressed in a mammalian cell line is transported into nuclei and is associated with intranuclear foci of condensed chromatin.  (+info)

Characterization of two related Drosophila gamma-tubulin complexes that differ in their ability to nucleate microtubules. (3/1790)

gamma-tubulin exists in two related complexes in Drosophila embryo extracts (Moritz, M., Y. Zheng, B.M. Alberts, and K. Oegema. 1998. J. Cell Biol. 142:1- 12). Here, we report the purification and characterization of both complexes that we name gamma-tubulin small complex (gammaTuSC; approximately 280,000 D) and Drosophila gammaTuRC ( approximately 2,200,000 D). In addition to gamma-tubulin, the gammaTuSC contains Dgrip84 and Dgrip91, two proteins homologous to the Spc97/98p protein family. The gammaTuSC is a structural subunit of the gammaTuRC, a larger complex containing about six additional polypeptides. Like the gammaTuRC isolated from Xenopus egg extracts (Zheng, Y., M.L. Wong, B. Alberts, and T. Mitchison. 1995. Nature. 378:578-583), the Drosophila gammaTuRC can nucleate microtubules in vitro and has an open ring structure with a diameter of 25 nm. Cryo-electron microscopy reveals a modular structure with approximately 13 radially arranged structural repeats. The gammaTuSC also nucleates microtubules, but much less efficiently than the gammaTuRC, suggesting that assembly into a larger complex enhances nucleating activity. Analysis of the nucleotide content of the gammaTuSC reveals that gamma-tubulin binds preferentially to GDP over GTP, rendering gamma-tubulin an unusual member of the tubulin superfamily.  (+info)

Cryoelectron microscopy of a nucleating model bile in vitreous ice: formation of primordial vesicles. (4/1790)

Because gallstones form so frequently in human bile, pathophysiologically relevant supersaturated model biles are commonly employed to study cholesterol crystal formation. We used cryo-transmission electron microscopy, complemented by polarizing light microscopy, to investigate early stages of cholesterol nucleation in model bile. In the system studied, the proposed microscopic sequence involves the evolution of small unilamellar to multilamellar vesicles to lamellar liquid crystals and finally to cholesterol crystals. Small aliquots of a concentrated (total lipid concentration = 29.2 g/dl) model bile containing 8.5% cholesterol, 22.9% egg yolk lecithin, and 68.6% taurocholate (all mole %) were vitrified at 2 min to 20 days after fourfold dilution to induce supersaturation. Mixed micelles together with a category of vesicles denoted primordial, small unilamellar vesicles of two distinct morphologies (sphere/ellipsoid and cylinder/arachoid), large unilamellar vesicles, multilamellar vesicles, and cholesterol monohydrate crystals were imaged. No evidence of aggregation/fusion of small unilamellar vesicles to form multilamellar vesicles was detected. Low numbers of multilamellar vesicles were present, some of which were sufficiently large to be identified as liquid crystals by polarizing light microscopy. Dimensions, surface areas, and volumes of spherical/ellipsoidal and cylindrical/arachoidal vesicles were quantified. Early stages in the separation of vesicles from micelles, referred to as primordial vesicles, were imaged 23-31 min after dilution. Observed structures such as enlarged micelles in primordial vesicle interiors, segments of bilayer, and faceted edges at primordial vesicle peripheries are probably early stages of small unilamellar vesicle assembly. A decrease in the mean surface area of spherical/ellipsoidal vesicles was correlated with the increased production of cholesterol crystals at 10-20 days after supersaturation by dilution, supporting the role of small unilamellar vesicles as key players in cholesterol nucleation and as cholesterol donors to crystals. This is the first visualization of an intermediate structure that has been temporally linked to the development of small unilamellar vesicles in the separation of vesicles from micelles in a model bile and suggests a time-resolved system for further investigation.  (+info)

Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. (5/1790)

The nucleocapsid of hepatitis B virus (HBV), or HBcAg, is a highly symmetric structure formed by multiple dimers of a single core protein that contains potent T helper epitopes in its 183-aa sequence. Both factors make HBcAg an unusually strong immunogen and an attractive candidate as a carrier for foreign epitopes. The immunodominant c/e1 epitope on the capsid has been suggested as a superior location to convey high immunogenicity to a heterologous sequence. Because of its central position, however, any c/e1 insert disrupts the core protein's primary sequence; hence, only peptides, or rather small protein fragments seemed to be compatible with particle formation. According to recent structural data, the epitope is located at the tips of prominent surface spikes formed by the very stable dimer interfaces. We therefore reasoned that much larger inserts might be tolerated, provided the individual parts of a corresponding fusion protein could fold independently. Using the green fluorescent protein (GFP) as a model insert, we show that the chimeric protein efficiently forms fluorescent particles; hence, all of its structurally important parts must be properly folded. We also demonstrate that the GFP domains are surface-exposed and that the chimeric particles elicit a potent humoral response against native GFP. Hence, proteins of at least up to 238 aa can be natively displayed on the surface of HBV core particles. Such chimeras may not only be useful as vaccines but may also open the way for high resolution structural analyses of nonassembling proteins by electron microscopy.  (+info)

Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation. (6/1790)

The interaction of foot-and-mouth disease virus (FMDV) serotype C (clone C-S8c1) with a strongly neutralising monoclonal antibody (MAb) 4C4 has been studied by combining data from cryoelectron microscopy and x-ray crystallography. The MAb 4C4 binds to the exposed flexible GH-loop of viral protein 1 (VP1), which appears to retain its flexibility, allowing movement of the bound Fab. This is in striking contrast to MAb SD6, which binds to the same GH-loop of VP1 but exhibits no movement of the bound Fab when observed under identical conditions. However, MAbs 4C4 and SD6 have very similar neutralisation characteristics. The known atomic structure of FMDV C-S8c1 and that of the 4C4 Fab cocrystallised with a synthetic peptide corresponding to the GH-loop of VP1 were fitted to the cryoelectron microscope density map. The best fit of the 4C4 Fab is compatible only with monovalent binding of the MAb in agreement with the neutralisation data on 4C4 MAbs, Fab2s, and Fabs. The position of the bound GH-loop is related to other known positions of this loop by a hinge rotation about the base of the loop. The 4C4 Fab appears to interact almost exclusively with the G-H loop of VP1, making no other contacts with the viral capsid.  (+info)

Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. (7/1790)

Herpes simplex virus type 1 virions were examined by electron cryomicroscopy, allowing the three-dimensional structure of the infectious particle to be visualized for the first time. The capsid shell is identical to that of B-capsids purified from the host cell nucleus, with the exception of the penton channel, which is closed. The double-stranded DNA genome is organized as regularly spaced ( approximately 26 A) concentric layers inside the capsid. This pattern suggests a spool model for DNA packaging, similar to that for some bacteriophages. The bulk of the tegument is not icosahedrally ordered. However, a small portion appears as filamentous structures around the pentons, interacting extensively with the capsid. Their locations and interactions suggest possible roles for the tegument proteins in regulating DNA transport through the penton channel and binding to cellular transport proteins during viral infection.  (+info)

Effect of buffer conditions on the position of tRNA on the 70 S ribosome as visualized by cryoelectron microscopy. (8/1790)

The effect of buffer conditions on the binding position of tRNA on the Escherichia coli 70 S ribosome have been studied by means of three-dimensional (3D) cryoelectron microscopy. Either deacylated tRNAfMet or fMet-tRNAfMet were bound to the 70 S ribosomes, which were programmed with a 46-nucleotide mRNA having AUG codon in the middle, under two different buffer conditions (conventional buffer: containing Tris and higher Mg2+ concentration [10-15 mM]; and polyamine buffer: containing Hepes, lower Mg2+ concentration [6 mM], and polyamines). Difference maps, obtained by subtracting 3D maps of naked control ribosome in the corresponding buffer from the 3D maps of tRNA.ribosome complexes, reveal the distinct locations of tRNA on the ribosome. The position of deacylated tRNAfMet depends on the buffer condition used, whereas that of fMet-tRNAfMet remains the same in both buffer conditions. The acylated tRNA binds in the classical P site, whereas deacylated tRNA binds mostly in an intermediate P/E position under the conventional buffer condition and mostly in the position corresponding to the classical P site, i. e. in the P/P state, under the polyamine buffer conditions.  (+info)

E3143-18b Standard Practice for Performing Cryo-Transmission Electron Microscopy of Liposomes vitrification~ transmission electron microscopes~
TY - JOUR. T1 - Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies. AU - Yu, Guimei. AU - Vago, Frank. AU - Zhang, Dongsheng. AU - Snyder, Jonathan E.. AU - Yan, Rui. AU - Zhang, Ci. AU - Benjamin, Christopher. AU - Jiang, Xi. AU - Kuhn, Richard J.. AU - Serwer, Philip. AU - Thompson, David H.. AU - Jiang, Wen. N1 - Funding Information: This work was supported in part by NIH Grant R01AI072035 . The negative staining TEM and cryo-EM images were taken at the Purdue Biological Electron Microscopy Facility. We thank Melissa Mikolaj and Thomas J. Edwards for providing some of the Sindbis virus test samples. PY - 2014/7. Y1 - 2014/7. N2 - Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies (i.e., protein complexes and viruses). Although single particle cryo-EM requires less concentrated and smaller amounts of samples than X-ray crystallography, it ...
ASSISTANT PROFESSOR IN CRYO ELECTRON MICROSCOPY in Full Time, Academia, Life Sciences with University of California, Irvine. Apply Today.
Single-particle cryo-electron microscopy has become an indispensable technique in structural biology. In particular when studying membrane proteins, it allows the use of membrane-mimicking tools,...
Author(s): Palovcak, Eugene Joseph | Advisor(s): Cheng, Yifan | Abstract: Biological macromolecules such as enzymes are nanoscale machines. This is true in a concrete sense: if the atomic structure of a biological macromolecule can be obtained, the theories of mechanics and intermolecular forces can be applied to explain how the machine works in terms that engineers would understand, including motors, ratchets, gates and transducers. Nevertheless, biological macromolecules are complex, fragile and extremely small, so obtaining their structures is a challenging experimental endeavor. Single-particle cryogenic electron microscopy (cryo-EM) is a technique for determining the 3D structure of a biological macromolecule from a large set of 2D electron micrographs of individual structurally-identical particles. To obtain such images, a solution of the macromolecules must be prepared in the frozen-hydrated state, embedded in a thin electron-transparent glassy film of water. This specimen must then be imaged
Link to Pubmed [PMID] - 27667334. Protein Sci. 2017 01;26(1):113-121. The tremendous pandemic potential of coronaviruses was demonstrated twice in the last 15 years by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor-binding and membrane fusion functions. Despite their biomedical importance, coronavirus S glycoproteins have proven difficult targets for structural characterization, precluding high-resolution studies of the biologically relevant trimer. Recent technological developments in single particle cryo-electron microscopy allowed us to determine the first structure of a coronavirus S glycoprotein trimer which provided a framework to understand the mechanisms of viral entry and suggested potential inhibition strategies for this family of viruses. Here, we describe the key factors that enabled this breakthrough.. https://www.ncbi.nlm.nih.gov/pubmed/27667334 ...
Abstract: We used cryogenic transmission electron microscopy (cryo-TEM) to identify differences in macromolecular structures present in the serum from healthy individuals (HI) and prostate cancer (PCa) patients and show that these differences are potential markers for disease. Using a murine orthotopic model of human PCa, we determined that some of these structural markers in serum are associated with the tumour burden. These findings signify the potential of this nanoscale ex vivo imaging technology of body fluids as a platform for discovering early markers of PCa and other diseases.. ...
Author(s): Jiang, Xi; Spencer, Ryan K; Sun, Jing; Ophus, Colin; Zuckermann, Ronald N; Downing, Kenneth H; Balsara, Nitash P | Abstract: Vesicle formation in a series of amphiphilic sequence-defined polypeptoid block co-polymers comprising a phosphonated hydrophilic block and an amorphous hydrophobic block, poly- N-(2-ethyl)hexylglycine- block-poly- N-phosphonomethylglycine (pNeh- b-pNpm), is studied. The hydrophobic/hydrophilic block ratio was varied keeping the total chain length of the co-polymers constant. A new approach for characterizing the vesicle membrane morphology based on low-dose cryogenic electron microscopy (cryo-EM) is described. The individual low-dose micrographs cannot be interpreted directly due to low signal-to-noise ratio. Sorting and averaging techniques, developed in the context of protein structure determination, were thus applied to vesicle micrographs. Molecular dynamic simulations of the vesicles were used to establish the relationship between membrane morphology and averaged
TY - JOUR. T1 - Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography. AU - Chiu, Wah. AU - Smith, Thomas. PY - 1994. Y1 - 1994. N2 - The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. Different kinds of viral proteins have been located and identified on the capsid surface, certain residues of the viral proteins involved in antibody interactions have been identified; the elbow angle of bound antibody has been measured; and the mechanism of antibody-mediated neutralization has been elucidated. Within the next few years, this combined methodology should help investigators resolve the structures of large macromolecular assemblies to even higher resolutions.. AB - The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Retroviral capsid proteins are conserved structurally but assemble into different morphologies. The mature human immunodeficiency virus-1 (HIV-1) capsid is best described by a fullerene cone model, in which hexamers of the capsid protein are linked to form a hexagonal surface lattice that is closed by incorporating 12 capsid-protein pentamers. HIV-1 capsid protein contains an amino-terminal domain (NTD) comprising seven α-helices and a β-hairpin, a carboxy-terminal domain (CTD) comprising four α-helices, and a flexible linker with a 310-helix connecting the two structural domains. Structures of the capsid-protein assembly units have been determined by X-ray crystallography; however, structural information regarding the assembled capsid and the contacts between the assembly units is incomplete. Here we report the cryo-electron microscopy structure of a tubular HIV-1 capsid-protein assembly at 8 Å resolution and the three-dimensional structure of a native HIV-1 core by cryo-electron tomography. The
Structural biology is undergoing a seismic shift as single-particle cryo-electron microscopy (cryo-EM) is increasingly becoming the technique of choice for scientists who want to study DNA, proteins and other biological molecules at atomic resolution. Having just recently broken the 3 Å (angstrom) barrier with the use of the Gatan K2 Summit® direct detection camera, a new structure shows that there is no longer a resolution gap between x-ray crystallography and cryo-EM.
Cullin-Ring E3 Ligases (CRLs) regulate a multitude of cellular pathways through specific substrate receptors. The COP9 signalosome (CSN) deactivates CRLs by removing NEDD8 from activated Cullins. Here we present structures of the neddylated and deneddylated CSN-CRL2 complexes by combining single-particle cryo-electron microscopy (cryo-EM) with chemical cross-linking mass spectrometry (XL-MS). These structures suggest a conserved mechanism of CSN activation, consisting of conformational clamping of the CRL2 substrate by CSN2/CSN4, release of the catalytic CSN5/CSN6 heterodimer and finally activation of the CSN5 deneddylation machinery. Using hydrogen-deuterium exchange (HDX)-MS we show that CRL2 activates CSN5/CSN6 in a neddylation-independent manner. The presence of NEDD8 is required to activate the CSN5 active site. Overall, by synergising cryo-EM with MS, we identify sensory regions of the CSN that mediate its stepwise activation and provide a framework for understanding the regulatory ...
Complex I (NADH:ubiquinone oxidoreductase), a major electron entry point to the mitochondrial respiratory chain, couples electron transfer from NADH to ubiquinone to proton pumping across the mitochondrial inner membrane, and generates the proton motive force that drives ATP synthesis and transport processes. The ~1 MDa mammalian complex contains 45 subunits, and pathological mutations in both its mitochondrial and nuclear encoded subunits result in diverse neuro-muscular disorders. Recent high-resolution mammalian complex I structures have been solved by single-particle cryo-electron microscopy (cryo-EM) in characterised biological states and provide mechanistic insights. However, the molecular bases of genetically-determined complex I dysfunctions remain unclear. Here, two mouse models of complex I-linked mitochondrial disease were analysed structurally by cryo-EM to understand the mechanisms of their pathogenesis. The first part of this thesis explores complex I from the ND6-P25 mouse model, ...
Magnesium ions are the most abundant divalent intracellular cations and are essential for life, as they play key roles in signaling, nucleic acid action and metabolism. Mg2+-deficiency is associated with diseases affecting the heart, muscle, bone, immune and nervous system, so it is very important to fully understand this ion uptake system. The ~200 kDa pentameric membrane channel CorA is the major Mg2+ uptake system in bacteria and a homolog of the eukaryotic mitochondrial Mrs2 proteins which it can complement. CorA contributes to Mg2+ homeostasis through a negative feedback loop, where Mg2+ binding at the subunit interface leads to channel closure and low Mg2+ concentrations stabilize the open conformation. Electron paramagnetic resonance (EPR) spectroscopic studies of purified CorA revealed large quaternary conformational changes associated with magnesium binding/unbinding. Using single-particle cryo-EM, we have determined the structure for the closed magnesium-bound state of CorA at a ...
Alon McCormick, course coordinator and IPrime NMP Program Leader. This course is intended to enable industrial and academic scientists and engineers with no prior knowledge of electron microscopy to gain insight into cryotechniques to image nanostructures in liquids, soft materials, and biological systems. After attending the course you will be better able to assess what experiments are feasible for samples of interest to you, and to estimate the benefits and costs of these approaches.. The main instructors are innovators and leaders in the field of cryo-electron microscopy, particularly in the study of soft materials, nanomaterials, and virus structure - Jayesh Bellare, Indian Institute of Technology, Bombay, Ishi Talmon, Technion, Israel Institute of Technology, Wei Zhang, U of MN CharFac & Institute for Molecular Virology.. Registration and fees ...
Addresses: UNIV PARIS SUD, EQUIPE PHYSICOCHIM SYST POLYPHASES, URA CNRS 1218, CHATENAY MALABRY, FRANCE. UNIV UPPSALA, INST PHYS CHEM, S-75121 UPPSALA, SWEDEN.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-03-21 ...
PhD Project - High resolution cryo-electron microscopy of clathrin cage networks at University of Warwick, listed on FindAPhD.com
TY - JOUR. T1 - Cryo-EM structure of oxysterol-bound human Smoothened coupled to a heterotrimeric Gi AU - Qi, Xiaofeng. AU - Liu, Heng. AU - Thompson, Bonne. AU - McDonald, Jeffrey. AU - Zhang, Cheng. AU - Li, Xiaochun. N1 - Publisher Copyright: © 2019, The Author(s), under exclusive licence to Springer Nature Limited.. PY - 2019/7/11. Y1 - 2019/7/11. N2 - The oncoprotein Smoothened (SMO), a G-protein-coupled receptor (GPCR) of the Frizzled-class (class-F), transduces the Hedgehog signal from the tumour suppressor Patched-1 (PTCH1) to the glioma-associated-oncogene (GLI) transcription factors, which activates the Hedgehog signalling pathway1,2. It has remained unknown how PTCH1 modulates SMO, how SMO is stimulated to form a complex with heterotrimeric G proteins and whether G-protein coupling contributes to the activation of GLI proteins3. Here we show that 24,25-epoxycholesterol, which we identify as an endogenous ligand of PTCH1, can stimulate Hedgehog signalling in cells and can trigger ...
TY - JOUR. T1 - Localization of eukaryote-specific ribosomal proteins in a 5.5-Å cryo-EM map of the 80S eukaryotic ribosome. AU - Armache, Jean Paul. AU - Jarasch, Alexander. AU - Anger, Andreas M.. AU - Villa, Elizabeth. AU - Becker, Thomas. AU - Bhushan, Shashi. AU - Jossinet, Fabrice. AU - Habeck, Michael. AU - Dindar, Gülcin. AU - Franckenberg, Sibylle. AU - Marquez, Viter. AU - Mielke, Thorsten. AU - Thomm, Michael. AU - Berninghausen, Otto. AU - Beatrix, Birgitta. AU - Söding, Johannes. AU - Westhof, Eric. AU - Wilson, Daniel N.. AU - Beckmann, Roland. PY - 2010/11/16. Y1 - 2010/11/16. N2 - Protein synthesis in all living organisms occurs on ribonucleoprotein particles, called ribosomes. Despite the universality of this process, eukaryotic ribosomes are significantly larger in size than their bacterial counterparts due in part to the presence of 80 r proteins rather than 54 in bacteria. Using cryoelectron microscopy reconstructions of a translating plant (Triticum aestivum) 80S ribosome ...
Posted on behalf of Elena Orlova... Dear All, It is a pleasure to announce that we are running the next EMBO practical course on image processing for cryo-electron microscopy in Birkbeck College , ISMB, London . This 10 day course will be held in September (5 - 15), 2017. You can find our announcement on the following sites: Twitter ( https://twitter.com/EMBOevents/status/818487485814730759 ), Facebook ( https://www.facebook.com/events/590421591166869/ ) EMBO events calendar ( http://www.embo.org/events/events-calendar ). Birkbeck College (http://www.bbk.ac.uk/biology/about-us/events/image-processing-for-cryo-electron-microscopy-1) Deadline for applications: Monday 15 May 2017 The aim of the course is to teach the basic principles and practical aspects of image processing to bioscientists and structural biologists wishing to determine macromolecular structures by cryo electron microscopy (EM). The course will concentrate on processing of single particle images, and will be aimed at advanced PhD ...
The Robert P. Apkarian Integrated Electron Microscopy Core (IECM) facility at Cherry Logan Emerson Hall is expanding to the O. Wayne Rollins Research Center, according to Assistant Dean of Research at the Emory University School of Medicine Michael E. Zwick. ... ...
Mucins are large glycoproteins that coat the surface of cells in the respiratory, digestive, and urogenital tracts. The first insights into the packing and secretion of intestinal MUC2 in molecular terms have now been obtained. Purified MUC2-N protein was analyzed by electron microscopy and image processing, suggesting how MUC2-N is packed in granulae of goblet cells. Dysregulation of the normal |1000-fold expansion upon release could explain the extreme viscosity of the produced mucus seen in cystic fibrosis.
Single particle cryoEM has emerged as a powerful method for structure determination of proteins and complexes, complementing X-ray crystallography and NMR spectroscopy. Yet, for many systems, the resolution of cryoEM density map has been limited to 4-6 Å, which only allows for resolving bulky amino acids side chains, thus hindering accurate model building from the density map. On the other hand, experimental chemical shifts (CS) from solution and solid state MAS NMR spectra provide atomic level data for each amino acid within a molecule or a complex; however, structure determination of large complexes and assemblies based on NMR data alone remains challenging. Here, we present a novel integrated strategy to combine the highly complementary experimental data from cryoEM and NMR computationally by molecular dynamics simulations to derive an atomistic model, which is not attainable by either approach alone. We use the HIV-1 capsid protein (CA) C-terminal domain as well as the large capsid assembly to
Single particle analysis is a group of related computerized image processing techniques used to analyze images from transmission electron microscopy (TEM). These methods were developed to improve and extend the information obtainable from TEM images of particulate samples, typically proteins or other large biological entities such as viruses. Individual images of stained or unstained particles are very noisy, and so hard to interpret. Combining several digitized images of similar particles together gives an image with stronger and more easily interpretable features. An extension of this technique uses single particle methods to build up a three-dimensional reconstruction of the particle. Using cryo-electron microscopy it has become possible to generate reconstructions with sub-nanometer resolution and near-atomic resolution first in the case of highly symmetric viruses, and now in smaller, asymmetric proteins as well. Single particle analysis can be done on both negatively stained and vitreous ...
The RyR1 acts as an intracellular calcium channel that allows passage of Ca2+ from the sarcoplasmic reticulum to the cytoplasm; this increase in cytosolic Ca2+ is required for excitation-contraction coupling. Certain mutations in RyR1 have been directly linked to malignant hyperthermia (MH) and central core disease. In a series of studies, the role of Mg2+ has been explored as it pertains to MH, and it has been determined that dysregulation of Mg2+ can even lead to MH in patients without mutations. Consequently, the aim of the study was to insert the RyR1 into nanodiscs, small, circular lipid bilayers used to solubilize membrane proteins, and to use cryo-electron microscopy to assess the conformation of the RyR1 in the presence of Mg2+ and AMP-PCP. Particle reconstruction generated a 9.0 Å resolution map that confirmed successful incorporation of the RyR1 into nanodiscs and allowed visualization of the RyR1 in a physiological closed state.
J Struct Biol. 2012 Jul;179(1):56-67. doi: 10.1016/j.jsb.2012.04.012. Epub 2012 May 1. Research Support, N.I.H., Extramural; Research Support, Non-U.S. Govt
Agenda. Webinar moderator: Patrick Schultz, IGBMC Strasbourg. Introduction - Integrated Structural Biology at the Centre for Integrative Biology / IGBMC. Speaker: Bruno Klaholz. Talk 1: Structural basis for the allosteric regulation of Human Topoisomerase 2α. Speaker: Valérie Lamour. Affiliation: IGBMC Strasbourg. Abstract: The human type IIA topoisomerases (Top2) are essential enzymes that regulate DNA topology and chromosome organization. The Top2α isoform is a prime target for antineoplastic compounds used in cancer therapy that form ternary cleavage complexes with the DNA. Despite extensive studies, structural information on this large dimeric assembly is limited to the catalytic domains, hindering the exploration of allosteric mechanism governing the enzyme activities. We produced the entire human Top2α in mammalian cells and present cryo-EM structures of the entire human Top2α nucleoprotein complex in different conformations at subnanometer resolutions. Our data unveils the molecular ...
So it is finally out: the cryoEM structure of Tet(O) on the ribosome we have collaborated on with Joachim Franks lab is finally published on in Nature Communications. Tet(O) is a bacterial translational GTPase that clears the ribosome from tetracycline antibiotic, and structural data provided in the paper shed light on the mechanism of Tet(O)-mediated resistance. Recently cryoEM of Tet(O)s close relative, Tet(M) was published by Beckmann and Wilson labs, so now one can compare the two. And yes, they look very similar. No surprise there. ...
Pre-mRNA splicing is executed by the spliceosome, which has eight major functional states each with distinct composition. Five of these eight human spliceosomal complexes, all preceding exon ligation, have been structurally characterized. In this study, we report the cryo-electron microscopy structures of the human post-catalytic spliceosome (P complex) and intron lariat spliceosome (ILS) at average resolutions of 3.0 and 2.9 Å, respectively. In the P complex, the ligated exon remains anchored to loop I of U5 small nuclear RNA, and the 3-splice site is recognized by the junction between the 5-splice site and the branch point sequence. The ATPase/helicase Prp22, along with the ligated exon and eight other proteins, are dissociated in the P-to-ILS transition. Intriguingly, the ILS complex exists in two distinct conformations, one with the ATPase/helicase Prp43 and one without. Comparison of these three late-stage human spliceosomes reveals mechanistic insights into exon release and spliceosome ...
Joachim Frank (Columbia University, New York, USA) is a pioneer of single particle reconstruction, which is the most used reconstruction method for 3DEM structures in EMDB and EM entries in PDB. And also, he is a develper of Spider, which is one of the most famous software in this field, and is used for some EM Navigor data (e.g. map projection/slice images ...
The use of 3D cryo-electron microscopy reconstruction (3DEM) methods to experimentally determine structures of biological macromolecules, complexes and machines is rapidly increasing in the structural biology community. For journal articles reporting new 3DEM structures via single particle, helical, electron crystallography, and sub-tomogram averaging methods, we find that the overall map-deposition rate to EM Data Bank (EMDB) is approaching 70%. However, the rate varies significantly per journal, and tends to be highest for journals with well-defined and consistently enforced 3DEM deposition policies in place ...
With our process, new types of proteins can be isolated from mixtures and characterized within a week, explains Daniel Rhinow from the Max Planck Institute of Biophysics. To date, just the isolation of the proteins was often part of a doctorate lasting several years. Together with Andreas Terfort (Goethe University Frankfurt) and Andrey Turchanin (Friedrich Schiller University Jena), the idea evolved a few years ago of fishing the desired proteins directly out of mixtures by equipping a nanosheet with recognition sites onto which the target protein bonds. The researchers have now succeeded in making proteins directly available for examination using electron cryo-microscopy through a smart nanosheet.. Cryo electron microscopy is based on the shock- reezing of a sample at temperatures below minus 150 degrees Celsius. During this process, the protein maintains its structure, no interfering fixing and coloring agents are needed, and the electrons can easily irradiate the frozen object. The ...
at the local three-fold axis in the cryoEM map was confirmed by mutagenesis to be essential for function. More recently, the cryo-EM structure of the tube was solved at 8Å resolution and this cryo-EM structure allowed unambiguous modeling and refinement by large-scale molecular dynamics (MD) simulation, resulting in all-atom models for the hexamer-of-hexamer and pentamer-of-hexamer elements of spheroidal capsids. Furthermore, the 3D structure of a native HIV-1 core was determined by cryo-electron tomography (Cryo-ET), which in combination with MD simulations permitted the construction of a realistic all-atom model for the entire capsid, based on the 3D authentic core structure. ...
I am the director of the newly founded Ernst-Ruska-Centre 3 for Structural Biology at the Forschungszentrum Jülich. I was a group leader at the EMBL from 2010 - 2018. I got in touch with electron cryomicroscopy by studying amyloid fibrils in the groups of Marcus Fändrich (now in Ulm, Germany) and Niko Grigorieff (now at Janelia Farm, USA).. For my postdoctoral period, I went to the MRC Laboratory of Molecular Biology (Cambridge, UK) to work with Richard Henderson and Roger Williams. In the last few years, we set up a group to study the mechanisms of autophagy by electron cryomicroscopy. Traditionally, I have been interested in the advancement of high-resolution single-particle EM with a particular focus on helical reconstruction. These developments have led to our recent helical processing software package Spring. More recently, we became interested in improving means of cryo-EM map interpretation by atomic models.. ...
Researchers at Osaka University used electron cryomicroscopy (CryoEM) to image essential cardiac muscle components, known as thin filaments, with unprecedented resolution. They also discovered the mechanism by which these filaments regulate heartbeat via cardiac muscle contractions in the presence or absence of calcium ions by changing their conformations.
US Air Force Research Lab. Monday, April 24, 2017, Colloquia Auditorium. Electron microscopy has been one of the robust tools in characterizing the life cycle of viruses, such as Semliki Forest Virus (SFV), an alphavirus that belongs to Togavirus family and causes encephalitis in human. The viral particle of SFV is composed of a nucleocapsid enclosed by a lipid-anchored glycoprotein spikes and infects cell through clathrin-dependent endocytosis pathway where it releases the nucleocapsid into the cytoplasm after membrane fusion at the late endosome. Cryo-electron microscopy and single particle reconstruction revealed the structure of SFV virion that both the nucleocapsid and surface spikes adapted into icosahedral symmetry with T4 surface lattice and that the connection between nucleocapsid protein and C-terminal tail of the glycoprotein stabilizes the particle integrity. Mutation at nucleocapsid does not changed the assembly of the viral particle although truncation at the RNA-binding domain ...
With the rapid progresses in both instrumentation and computing, it is increasingly straightforward and routine to determine the structures of icosahedral viruses to subnanometer resolutions (6-10 Å)...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Zinc atom in PDB 3dco: Drosophila Nod (3DC4) and Bovine Tubulin (1JFF) Docked Into The 11-Angstrom Cryo-Em Map of Nucleotide-Free Nod Complexed to the Microtubule
by Victor A. Kostyuchenko, Elisa X. Y. Lim, Shuijun Zhang, Guntur Fibriansah, Thiam-Seng Ng, Justin S. G. Ooi, Jian Shi & Shee-Mei Lok. Nature (2016) doi:10.1038/nature17994 Published online 19 April 2016. Zika virus (ZIKV), formerly a neglected pathogen, has recently been associated with microcephaly in fetuses1, and with Guillian-Barré syndrome in adults2. Here we present the 3.7 Å resolution cryo-electron microscopy structure of ZIKV, and show that the overall architecture of the virus is similar to that of other flaviviruses. Sequence and structural comparisons of the ZIKV envelope (E) protein with other flaviviruses show that parts of the E protein closely resemble the neurovirulent West Nile and Japanese encephalitis viruses, while others are similar to dengue virus (DENV). However, the contribution of the E protein to flavivirus pathobiology is currently not understood. The virus particle was observed to be structurally stable even when incubated at 40 °C, in sharp contrast to the less ...
Pathological protein clumps are characteristic of a series of diseases, such as Alzheimers disease, Parkinsons disease, and type 2 diabetes. Scientists at Forschungszentrum Jülich, Heinrich Heine University Düsseldorf, and Maastricht University have now used cryo-electron microscopy to obtain a sharp image for the first time of how individual molecules are arranged in protein strings, which constitute the deposits typical for diabetes. The structure of the fibrils is very similar to that of Alzheimers fibrils.
Scientists have used cryo-electron microscopy to capture the first atomic-level images of the crystalline dendrites that can grow in batteries.
The 9 Å resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180^o and to move away from the center of the spikes during fusion. ...
Cryo-electron microscopy (cryo-EM) is a structural technique that images biological macromolecules in native-like conditions, and has been widely applied to the study of viruses. Virus structures have been determined by cryo-EM at resolutions ranging from molecular (~30-50Angstrom) to near atomic (~4 angstrom).... ...
Most fellows will come directly from a PhD or MD program and have expertise in a wide range of innovative technologies. Their work will have a combination of novelty, originality and risk, factors that often lower the chances of obtaining support through traditional channels. Salk Fellows will be independent group leaders and will be appointed for an initial period of three years, which may be followed by a two-year extension.. Salks first Fellow in this new program, Dmitry Lyumkis, joined the Salk on July 1 from The Scripps Research Institute and has made groundbreaking innovations in biological imaging. He uses single-particle cryo-electron microscopy-a cutting-edge technology that enables the visualization of large proteins and protein complexes under near-native conditions-to build three-dimensional models of the imaged objects. The resulting 3D models, which can now be resolved at near-atomic resolution with select specimens, facilitate a better understanding of protein function and ...
Eukaryotic origins of replication are licensed upon loading of the MCM helicase motor onto DNA. ATP hydrolysis by MCM is required for loading and the post-catalytic MCM is an inactive double hexamer that encircles duplex DNA. Origin firing depends on MCM engagement of Cdc45 and GINS to form the CMG holo-helicase. CMG assembly requires several steps including MCM phosphorylation by DDK. To understand origin activation, here we have determined the cryo-EM structures of DNA-bound MCM, either unmodified or phosphorylated, and visualize a phospho-dependent MCM element likely important for Cdc45 recruitment. MCM pore loops touch both the Watson and Crick strands, constraining duplex DNA in a bent configuration. By comparing our new MCM-DNA structure with the structure of CMG-DNA, we suggest how the conformational transition from the loaded, post-catalytic MCM to CMG might promote DNA untwisting and melting at the onset of replication. ...
FEI have recently collaborated with the ARC Centre of Excellence in Advanced Molecular Imaging (Imaging CoE) to test a new approach to optimise samples prior to preparing them for vitrification and subsequent cryo-transmission electron microscopy (cryo-EM).
Fingerprint Dive into the research topics of Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Together they form a unique fingerprint. ...
The blood-sucking reduviid bug Triatoma infestans, one of the most important vector of American human trypanosomiasis (Chagas disease) is infected by the Triatoma virus (TrV). TrV has been classified as a member of the Cripavirus genus (type cricket paralysis virus) in the Dicistroviridae family. This work presents the three-dimensional cryo-electron microscopy (cryo-EM) reconstruction of the TrV capsid at about 25 A resolution and its use as a template for phasing the available crystallographic data by the molecular replacement method. The main structural differences between the cryo-EM reconstruction of TrV and other two viruses, one from the same family, the cricket paralysis virus (CrPV) and the human rhinovirus 16 from the Picornaviridae family are presented and discussed.
Cryo electron microscopy and electron tomography will play a crucial role in the future of drug development.. The completion of the human genome project has focused tremendous interest in determining the structure and function of the tens of thousands of proteins that the genome encodes. Current structural determination techniques are difficult, time-consuming and not generally applicable to all proteins.. Cryo Electron Tomography (ET) is, by comparison, relatively straightforward and fast. While it does not achieve atomic scale resolution, it can resolve tertiary and quaternary structure - the level at which much of the critical interaction between proteins occurs. Because it does not require crystallisation, it is applicable to most proteins, including large proteins and protein complexes, flexible proteins and membrane proteins. Because it operates on a single protein molecule, it can provide information that is critical to drug development and unavailable from other techniques, for example, ...
Author: Lucic, V. et al.; Genre: Journal Article; Published in Print: 2008-08; Keywords: cryo-electron tomography; correlative light microscopy; electron microscopy; Title: Cryo-electron tomography of cells: connecting structure and function
Combined Cryogenic Transmission Electron Microscopy and Electron Spin Resonance Studies of Egg Phosphatidylchloline Liposomes Loaded with a Carboranyl Compound Intended for Boron Neutron Capture Therapy ...
Foamy viruses (FV) belong to the genus Spumavirus, which forms a distinct lineage in the Retroviridae family. Although the infection in natural hosts and zoonotic transmission to humans is asymptomatic, FVs can replicate well in human cells making it an attractive gene therapy vector candidate. Here we present cryo-electron microscopy and (cryo-)electron tomography ultrastructural data on purified prototype FV (PFV) and PFV infected cells. Mature PFV particles have a distinct morphology with a capsid of constant dimension as well as a less ordered shell of density between the capsid and the membrane likely formed by the Gag N-terminal domain and the cytoplasmic part of the Env leader peptide gp18LP. The viral membrane contains trimeric Env glycoproteins partly arranged in interlocked hexagonal assemblies. In situ 3D reconstruction by subtomogram averaging of wild type Env and of a Env gp48TM- gp80SU cleavage site mutant showed a similar spike architecture as well as stabilization of the hexagonal
The Nobel prize in chemistry has been awarded to the three scientists for developing a technique to produce images of the molecules of life frozen in time. The technique, called cryo-electron microscopy, allows biomolecules to be visualised in their natural configuration for the first time, triggering a revolution in biochemistry, according to the Nobel committee. The latest versions of the technology mean scientists can record biochemical processes as they unfold in film-like sequences.. Richard Henderson, a Scottish scientist and professor at the MRC Laboratory of Molecular Biology, was the first to successfully modify the electron microscope to image a protein involved in photosynthesis, by using a weaker beam and taking pictures from many angles. Joachim Frank, a German-born professor at Columbia University in New York, developed mathematical algorithms that allowed the method to be applied to a wider array of molecules. Jacques Dubochet, who is Swiss and an honorary professor at the ...
Bunyaviridae is a large family of viruses that have gained attention as emerging viruses because many members cause serious disease in humans, with an increasing number of outbreaks. These negative-strand RNA viruses possess a membrane envelope covered by glycoproteins. The virions are pleiomorphic and thus have not been amenable to structural characterization using common techniques that involve averaging of electron microscopic images. Here, we determined the three-dimensional structure of a member of the Bunyaviridae family by using electron cryotomography. The genome, incorporated as a complex with the nucleoprotein inside the virions, was seen as a thread-like structure partially interacting with the viral membrane. Although no ordered nucleocapsid was observed, lateral interactions between the two membrane glycoproteins determine the structure of the viral particles. In the most regular particles, the glycoprotein protrusions, or spikes, were seen to be arranged on an icosahedral ...
cryo-electron tomography | This blog addresses the various applications and techniques to be discovered in the fields of cathodoluminescence and correlative light and electron microscopy.
We and others recently developed rapid tilt-series acquisition methods for cryo-electron tomography on a Titan Krios G3i equipped with a single axis holder and a K-series direct electron detector and showed that one of these, the fast-incremental single exposure (FISE) method, significantly accelerates tilt-series acquisition when compared to traditional methods while preserving the quality of the images. Here, we characterize the behavior of our single axis holder in detail during a FISE experiment to optimally balance data quality with speed. We explain our methodology in detail so others can characterize their own stages, and conclude with recommendations for projects with different resolution goals. ...
Cryo-electron tomography is an important tool to study structures of macromolecular complexes in close to native states. A whole cell cryo electron tomogram contains structural information of all its macromolecular complexes. However, extracting this information remains challenging, and relies on sophisticated image processing, in particular for template-free particle extraction, classification and averaging. To develop these methods it is crucial to realistically simulate tomograms of crowded cellular environments, which can then serve as ground truth models for assessing and optimizing methods for detection of complexes in cell tomograms. We present a framework to generate crowded mixtures of macromolecular complexes for realistically simulating cryo electron tomograms including noise and image distortions due to the missing-wedge effects. Simulated tomograms are then used for assessing the template-free Difference-of-Gaussian (DoG) particle-picking method to detect complexes of different shapes and
Now we can see the intricate details of the biomolecules in every corner of our cells, in every drop of our body fluids, says Sara Snogerup Linse, a Swedish scientist who chairs the Nobel committee for chemistry. Frank, who was born in Germany during World War II, received degrees from the Universities of Freiburg and Munich before earning a doctorate in physics from the Technical University of Munich in 1970. Over the next few decades, he held positions at a number of academic institutions in Germany, the United Kingdom, and the United States, all the while researching the computational-imaging methods that eventually made cryo-electron microscopy possible. He joined Columbia as a professor in the Department of Biochemistry and Molecular Biophysics and the Department of Biological Sciences in 2008. In his own research, Frank has used cryo-electron microscopy to investigate the interactions between ribosomes - which serve as the protein factories of the cell - and other molecules. In a 2013 ...
Gag, the major structural component of the type 1 human immunodeficiency virus (HIV-1), comprises the matrix (MA), capsid (CA), nucleocapsid (NC), and p6 proteins, as well as the SP1 and SP2 spacer peptides. In the immature HIV-1 virion, the domains of Gag are arranged radially with the amino-terminus of MA at the membrane. Mature viral particles are formed when Gag is proteolytically cleaved, allowing CA to reassemble into the viral core, which contains NC bound to genomic RNA. While the structures of nearly every HIV-1 protein are known in atomic detail from X-ray crystallography and NMR spectroscopy, many questions remain about the intermolecular interactions in both the immature and mature particles. We have obtained three-dimensional structures of individual immature and mature HIV-1 virus-like particles by cryoelectron tomography. Reconstructions of the mature particles revealed diverse core morphologies with a preference for conical shapes consistent with 5,7 fullerene cones. Uniform ...
Dearborn AD, Wall JS, Cheng N, Heymann JB, Kajava AV, Varkey J, Langen R, Steven AC (2016) Alpha-synuclein amyloid fibrils with two entwined, asymmetrically associated protofibrils. J Biol Chem. 291(5): 2310 - 2318.. DiMattia MA, Watts NR, Cheng N, Huang R, Heymann JB, Grimes JM, Wingfield PT, Stuart DI, Steven AC (2016) The structure of hiv-1 rev filaments suggests a bilateral model for rev-rre assembly. Structure. 24(7): 1068 - 1080.. Fontana J, Cardone G, Heymann JB, Winkler DC and Steven AC (2012) Structural Changes in Influenza Virus at Low pH Characterized by Cryo-Electron Tomography. Journal of Virology, 86(6): 2919 - 2929.. Grünewald K, Desai P, Winkler DC, Heymann JB, Belnap DM, Baumeister W and Steven AC (2003). Three-dimensional structure of herpes simplex virus from cryo-electron tomography. Science 302(5649): 1396 - 1398.. Harris A, Cardone G, Winkler DC, Heymann JB, Brecher M, White JM, Steven AC (2006) Influenza virus pleiomorphy characterized by cryoelectron tomography. ...
The basic principle of electron crystallography is to calculate a 3D density map by combining the amplitudes obtained from electron diffraction patterns with the experimental phases calculated from images of two-dimensional crystals of membrane or soluble proteins. This technology is very well developed and has produced a number of atomic models of membrane proteins in a lipid environment. Focused on comprehensive experimental protocols, Electron Crystallography of Soluble and Membrane Proteins: Methods and Protocols covers the entire range of techniques used in electron crystallography, including protein sample preparation, 2D crystallization, and screening in negative stain over electron cryo-microscopy (cryo-EM) and data processing, as well as modeling of conformational changes. Additional chapters provide perspective on past, present, and future challenges as well as complementary methods. Written for the popular Methods in Molecular Biology™ series, the work contains the kind of detailed ...
Oda and Yanagisawa report 3D cryo-electron tomography structures of Z-disc from porcine cardiac myofibrils in relaxed and activated states. They show that α-actinin dimers exhibit contraction dependent swinging and sliding motions in response to a global twist in the F-actin lattice. These findings provide insights into conformational changes of the Z-disc in the context of active myofibrils.. ...
The 5-untranslated region of the hepatitis C virus genome contains an internal ribosome entry site (IRES) that initiates cap-independent translation of the viral RNA. Until now, the structural characterization of the entire (IRES) remained limited to cryo-electron microscopy reconstructions of the (IRES) bound to different cellular partners. Here we report an atomic model of free full-length hepatitis C virus (IRES) refined by selection against small-angle X-ray scattering data that incorporates the known structures of different fragments. We found that an ensemble of conformers reproduces small-angle X-ray scattering data better than a single structure suggesting in combination with molecular dynamics simulations that the hepatitis C virus (IRES) is an articulated molecule made of rigid parts that move relative to each other. Principal component analysis on an ensemble of physically accessible conformers of hepatitis C virus (IRES) revealed dominant collective motions in the molecule, which may
Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the FO region support a Brownian ratchet mechanism for proton-translocation-driven rotation in ATP synthases.. ...
The structure of a TMEM16 scramblase, which functions as a lipid transporter and plays an important role in blood coagulation, was already known from previous work. Researchers of the Department of Biochemistry at the University of Zurich have now also succeeded in decrypting the structure of the chloride channel TMEM16A. To do so, the team led by Professor Raimund Dutzler used cryo-electron microscopy (cryo-EM), a technique whose pioneers were recently awarded the Nobel Prize in Chemistry. The molecular architecture of this membrane protein is crucial for the targeted development of drugs for treating cystic fibrosis, emphasizes Dutzler.. Discovery of a novel activation mechanism. The chloride channel TMEM16A can be found in different organs of the body and plays a key role in the secretion of chloride in the lung, the contraction of smooth muscles, and the perception of pain. How its structure differs from closely related scramblases of the same family and how the protein is activated by ...
Author: Walz, J. et al.; Genre: Journal Article; Published in Print: 1999; Keywords: Electron microscopy; Icosahedral capsids; Image analysis; Thermoplasma.; Degradation; Microscopy; Resolution; Products.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.; Title: Capsids of tricorn protease studied by electron cryomicroscopy
The investigation of the coacervation (self-aggregation) behavior of biomicrogels which can potentially be used as drug carriers is an important topic, because self-aggregation can not only cause loss of activity, but also toxicity and immunogenicity. To study this effect microgels from elastin-like recombinamer are synthesized using miniemulsion technique. The existence of coacervation for such microgels, at different concentrations and temperatures, is studied and proved by cryo-field emission scanning clectron microscopy (cryo-FESEM), cryo-transmission electron microscopy (cryo-TEM), and by a novel 1H high-resolution magic angle sample spinning (HRMAS), nuclear magnetic resonance (NMR) spectroscopy, and relaxometry methods. The findings by 1H HRMAS NMR spectroscopy and relaxometry show simultaneous processes of volume phase temperature transition and coacervation with different sensitivity for hydrophobic and hydrophilic amino acid side-chains in the microgel. The coacervation process is more ...
Related Articles Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome. Proc Natl Acad Sci U S A. 2014 May 20;111(20):7284-9 Authors: Kaushal PS, Sharma MR, Booth TM, Haque EM, Tung CS, Sanbonmatsu KY, Spremulli LL, Agrawal RK Abstract The mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing 13 membrane proteins that form…
High axial aspect crystalline nanomaterials have emerged as polymeric building blocks for the construction of supermaterials. In contrast to this form, amorphous nanospheres have remained largely untapped. This is especially peculiar in the context of material assembly, due to the wide range of opportunities they offer by virtue of their soft particle characteristics, high volume ratio at low solid content and their highly swollen and accessible structure. In the context of cellulose, these colloids represent a new field in the family of nanocelluloses. We report an organic solvent-free, heterogeneous and simple synthesis of spherical carboxylated nanoparticles bearing a distinctive, amorphous outer shell structure. The particle shape is evaluated by atomic force microscopy, cryo-transmission electron microscopy, dynamic light scattering and small-angle X-ray scattering. The soft shell structure of the particles and their responsiveness to ionic strength and pH are quantified by the combination ...
Cryo-Electron Three-Dimensional Imaging of Soft Materials. Cryogenic transmission electron microscopy (Cryo-TEM) is used to characterize labile systems that are not allowed in room temperature electron microscopy due to a high vapor pressure. Although soft materials are characterized with cryo-TEM, the original structure of the sample is lost. This is because a three-dimensional (3D) structure is projected to a two-dimensional (2D) image. These researchers used a single-particle construction method to visualize conventional 2D images to 3D microstructures with a high resolution. They are exploring an electron tomography method to construct 3D images. This method combines a series of 2D images that are collected at different angles and constructs a 3D image. To do this, mathematical algorithms of cross-correlation and an image alignment must be combined and solved simultaneously. Computer calculations are indispensable in structure characterization study and allow researchers to understand the ...
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I am professor in electron cryotomography and bacterial chemotaxis. I am interested in understanding how microbes sense and respond to their environment. In order to gain insight into the structure and function of the molecular complexes involved in these behaviors, my lab uses electron cryotomography (ECT). This technique allows us to directly study microbes in their native state at resolutions capable of visualizing individual proteins.
Mimivirus, Acanthamoeba polyphaga, cryo-electron microscope, Atomic Force Microscope, fiber, DIGESTION, starfish-shaped feature, 5-fold symmetry, nucleocapsid, major capsid ...
Sindbis virus (SINV) is an enveloped, mosquito-borne alphavirus. Here we generated and characterized a fluorescent protein-tagged (FP-tagged) SINV and found that the presence of the FP-tag (mCherry) affected glycoprotein transport to the plasma membrane whereas the specific infectivity of the virus was not affected. We examined the virions by transmission electron cryo-microscopy and determined the arrangement of the FP-tag on the surface of the virion. The fluorescent proteins are arranged icosahedrally on the virus surface in a stable manner that did not adversely affect receptor binding or fusion functions of E2 and E1, respectively. The delay in surface expression of the viral glycoproteins, as demonstrated by flow cytometry analysis, contributed to a 10-fold reduction in mCherry-E2 virus titer. There is a 1:1 ratio of mCherry to E2 incorporated into the virion, which leads to a strong fluorescence signal and thus facilitates single-particle tracking experiments. We used the FP-tagged virus for high
ATP, the universal energy currency of cells, is produced by F-type ATP synthases, which are ancient, membrane-bound nanomachines. F-type ATP synthases use the energy of a transmembrane electrochemical gradient to generate ATP by rotary catalysis. Protons moving across the membrane drive a rotor ring composed of 8-15 c-subunits. A central stalk transmits the rotation of the c-ring to the catalytic F1 head, where a series of conformational changes results in ATP synthesis. A key unresolved question in this fundamental process is how protons pass through the membrane to drive ATP production. Mitochondrial ATP synthases form V-shaped homodimers in cristae membranes. Here we report the structure of a native and active mitochondrial ATP synthase dimer, determined by single-particle electron cryomicroscopy at 6.2 Å resolution. Our structure shows four long, horizontal membrane-intrinsic α-helices in the a-subunit, arranged in two hairpins at an angle of approximately 70° relative to the c-ring ...
Telomeres are large nucleoproteins structures that cap the ends of chromosomes in eukaryotic cells. When a cell divides, a small portion of the telomere is lost due to the inherently incomplete process of genome replication. If left unchecked, over time the telomeres will reach a critically short length and the cell will face genomic instability, deterioration or death. To offset this shortening, an essential enzyme called telomerase rebuilds the telomeres by synthesizing new telomeric DNA repeats at chromosome ends. Kelly Nguyens group, in the LMBs Structural Studies Division, has solved the first complete atomic model of this enzyme and discovered a histone dimer as novel telomerase subunits.
December 9th, 2019 by Dirksen E. Bussiere. Nature Chemical Biology, Published online: 09 December 2019; doi:10.1038/s41589-019-0411-6. The crystal and cryo-electron microscopy structure analysis of the DCAF15-DDB1-DDA1-indisulam-RBM39 complex revealed the detailed mechanism of action of indisulam-induced RBM39 degradation and defined an α-helical degron motif in RBM39 ...
Miller, A. N.*, Vaisey, G.*, & Long, S. B. (2019). Molecular mechanisms of gating in the calcium-activated chloride channel bestrophin. eLife (Abstract , open state Cryo-EM map , Atomic Coordinates). *A. N. Miller and G. Vaisey are co-first authors.. Vaisey, G., & Long, S. B. (2018). An allosteric mechanism of inactivation in the calcium-dependent chloride channel BEST1. The Journal of General Physiology, jgp.201812190. (Abstract). Hou, X., Burstein, S. R., & Long, S. B. (2018). Structures reveal opening of the store-operated calcium channel Orai. eLife, 7. (Manuscript , Atomic Coordinates). Baradaran, R., Wang, C., Siliciano, A. F., & Long, S. B. (2018). Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters. Nature, 559(7715), 580-584. (Abstract , Atomic Coordinates , Cryo-EM map). Melinda Diver, Leanne Pedi, Akiko Koide, Shohei Koide, Stephen B. Long (2018). Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT. Nature. Jan 25; 553(7689):526-529. ...
The issue of protein dynamics and its implications in the biological function of proteins are arousing greater and greater interest in different fields of molecular biology. In cryo-electron tomography experiments one may take several snapshots of a given biological macromolecule. In principle, a large enough collection of snapshots of the molecule may then be used to calculate its equilibrium configuration in terms of the experimentally accessible degrees of freedom and, hence, to estimate its potential energy. This information would be crucial in order to analyze the biological functions of biomolecules by directly accessing the relevant dynamical indicators. In this article, we analyze the results of cryo-electron tomography experiments performed on monoclonal murine IgG2a antibodies. We measure the equilibrium distribution of the molecule in terms of the relevant angular coordinates and build a mechanical model of the antibody dynamics. This approach enables us to derive an explicit ...
For example, the researchers now know that most of the fibers are usually bound to the virus head rather than extended, as was previously thought. That those fibers are in a dynamic equilibrium between bound and extended states is also new. Molineux said that the idea that phages walk over the cell surface was previously proposed, but their paper provides the first experimental evidence that this is the case. This is also the first time that scientists have made actual images showing how the viruss tail extends into the host - the very action that allows it to infect a cell with its DNA.. I first hypothesized that T7 made an extended tail more than 10 years ago, said Molineux, but this is the first irrefutable experimental evidence for the idea and provides the first images of what it looks like.. The researchers used a combination of genetics and cryo-electron tomography to image the infection process. Cryo-electron tomography is a process similar to a CT scan, but it is scaled to study ...
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ALA is a plant-derived n-3 FA readily available in certain plant oils such as flaxseed, soybean and canola oil. Epidemiological studies have shown an inverse correlation between dietary ALA and cardiovascular events,11,30,31 although the molecular mechanisms of this protection are not completely known. Our group has investigated the molecular basis of several cardio-protective effects of ALA, showing that at least some of its effects are mediated by its action on endothelial cells, leukocytes and platelets.9,10,19 In this study, we have focused in particular on platelet adhesion to vWF under high-shear conditions, which represents the first step mediating platelet activation under arterial flow and is especially important in stenosed (atherosclerotic) arteries, where shear can reach extremely high values (,5,000 s−1).7,32,33. Here we show for the first time that ALA is able to partially inhibit platelet adhesion to vWF under a shear flow of 10,000 s−1, when whole blood is pre-incubated for 1 ...
The new LSV laser-interferometric vibrometer is the ideal instrument for accurate, non-contact determination of temporal changes in the positions of objects or surfaces of arbitrary roughness
Biology is a challenging and complicated mess. Understanding this challenging complexity is the realm of the biological sciences: Trying to make sense of the massive, messy data in terms of discovering patterns and revealing its underlying general rules. Among the most powerful mathematical tools for organizing and helping to structure complex, heterogeneous and noisy data are the tools provided by multivariate statistical analysis (MSA) approaches. These eigenvector/eigenvalue data-compression approaches were first introduced to electron microscopy (EM) in 1980 to help sort out different views of macromolecules in a micrograph. After 35 years of continuous use and developments, new MSA applications are still being proposed regularly. The speed of computing has increased dramatically in the decades since their first use in electron microscopy. However, we have also seen a possibly even more rapid increase in the size and complexity of the EM data sets to be studied. MSA computations had thus become a
Heterotrimeric AMP-activated protein kinase (AMPK) is crucial for energy homeostasis of eukaryotic cells and organisms. Here we report on (i) bacterial expression of untagged mammalian AMPK isoform combinations, all containing gamma(1), (ii) an automated four-dimensional purification protocol, and (iii) biophysical characterization of AMPK heterotrimers by small angle x-ray scattering in solution (SAXS), transmission and scanning transmission electron microscopy (TEM, STEM), and mass spectrometry (MS). AMPK in solution at low concentrations (~1 mg/ml) largely consisted of individual heterotrimers in TEM analysis, revealed a precise 1:1:1 stoichiometry of the three subunits in MS, and behaved as an ideal solution in SAXS. At higher AMPK concentrations, SAXS revealed concentration-dependent, reversible dimerization of AMPK heterotrimers and formation of higher oligomers, also confirmed by STEM mass measurements. Single particle reconstruction and averaging by SAXS and TEM, respectively, revealed similar
We demonstrate the use of a hole-free phase plate (HFPP) for magnetic imaging in transmission electron microscopy by mapping the domain structure in PrDyFeB samples. The HFPP, a Zernike-like imaging method, allows for detecting magnetic signals in-focus to correlate the sample crystal structure and defects with the local magnetization topography, and to evidence stray fields protruding from the sample. Experimental and simulated results are shown and are compared with conventional Fresnel (out-of-focus) images without a phase plate. A key advantage of HFPP imaging is that the technique is free from the reference wave distortion from long-range fields affecting electron holography ...
Cryo-Electron Microscopy (cryo-EM) is an imaging technology that is revolutionizing structural biology; the Nobel Prize in Chemistry 2017 was recently awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution.. Cryo-electron microscopes produce a large number of very noisy two-dimensional projection images of individual frozen molecules. Unlike related methods, such as computed tomography (CT), the viewing direction of each image is unknown. The unknown directions, together with extreme levels of noise and additional technical factors, make the determination of the structure of molecules challenging.. While other methods for structure determination, such as x-ray crystallography and nuclear magnetic resonance (NMR), measure ensembles of molecules, cryo-electron microscopes produce images of individual molecules. Therefore, cryo-EM could potentially be used to study ...
Ribosomes are large ribonucleoprotein complexes which incorporate amino acids into peptide chains during translational process in all types of living cells. The eukaryotic ribosome is larger compared to its prokaryotic counterpart. The size differences are due to a larger protein part and that the rRNA contains eukaryote specific expansion segments (ES). Cryo-EM reconstruction has visualized many ES on the ribosomal surface which have given clues about function and structural features. However, the secondary structures of most ES are unknown or ill defined. In this thesis, the secondary and also to a certain extent the tertiary structures of several ES are determined by using computational methods and biochemical experimental techniques. The juxtaposition of ES6 close to ES3 in the Cryo-EM image of the yeast ribosome suggested that ES3 and ES6 might interact. A computational analysis of more than 2900 sequences shows that a complementary helical region of seven to nine contiguous base pairs can ...
Title: Inverse Problems and Unsupervised Learning with applications to Cryo-Electron Microscopy (cryo-EM) Abstract: Cryo-EM is an imaging technology that is revolutionizing structural biology; the Nobel Prize in Chemistry 2017 was recently awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution. Cryo-electron microscopes produce a large number of very noisy two-dimensional projection images of individual frozen molecules. Unlike related methods, such as computed tomography (CT), the viewing direction of each image is unknown. The unknown directions, together with extreme levels of noise and additional technical factors, make the determination of the structure of molecules challenging. While other methods for structure determination, such as x-ray crystallography and nuclear magnetic resonance (NMR), measure ensembles of molecules together, cryo-EM produces measurements ...
Title: Inverse Problems and Unsupervised Learning with applications to Cryo-Electron Microscopy (cryo-EM) Abstract: Cryo-EM is an imaging technology that is revolutionizing structural biology; the Nobel Prize in Chemistry 2017 was recently awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution. Cryo-electron microscopes produce a large number of very noisy two-dimensional projection images of individual frozen molecules. Unlike related methods, such as computed tomography (CT), the viewing direction of each image is unknown. The unknown directions, together with extreme levels of noise and additional technical factors, make the determination of the structure of molecules challenging. While other methods for structure determination, such as x-ray crystallography and nuclear magnetic resonance (NMR), measure ensembles of molecules together, cryo-EM produces measurements ...

No data available that match "cryoelectron microscopy"


... but it is systematically excluded from conventional electron microscopy. This is because water evaporates rapidly under the ... Lepault J (1985) Cryo-electron microscopy of helical particles TMV and T4 polyheads. J Microsc (Oxford) 140:73-80.CrossRef ... McDowall AW, Smith JM, Dubochet J (1986) Cryo-electron microscopy of vitrified chromosomes in situ. EMBO J 5:1395-1402.PubMed ... Cryoelectron microscopy has long been seen as a possible avenue to overcome this limitation, but until recently the direct ...
... critical to the advance of cryo-electron microscopy, allowing researchers to obtain images of biological materials that more ... he continued to refine techniques for structural imaging of biological materials by cryo-electron microscopy. He developed a ... Other articles where Cryo-electron microscopy is discussed: Jacques Dubochet: … ... using a technique known as cryo-electron microscopy. Hendersons refinement of imaging methods for cryo-electron microscopy, in ...
Computational Reconstruction in Cryo-Electron Microscopy Computational Reconstruction in Cryo-Electron Microscopy ... and extract the inherent molecular flexibility and motions from the cryo-electron micrographs. Finally, I will describe some ...
Jiang W., Chiu W. (2007) Cryoelectron Microscopy of Icosahedral Virus Particles. In: Kuo J. (eds) Electron Microscopy. Methods ... 1988) Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys. 21, 129-228.PubMedCrossRefGoogle Scholar ... Adrian, M., Dubochet, J., Lepault, J., and McDowall, A. W. (1984) Cryo-electron microscopy of viruses. Nature 308, 32-36.PubMed ... Cryo-EM cryoelectron microscopy icosahedral virus 3D reconstruction subnanometer resolution secondary structure elements ...
The acquisition of cryo-electron microscopy (cryo-EM) data from biological specimens must be tightly coupled to data ... Real-time cryo-electron microscopy data preprocessing with Warp. *Dimitry Tegunov. ORCID: orcid.org/0000-0001-7019-32211. & ... Saibil, H. R., Grünewald, K. & Stuart, D. I. A national facility for biological cryo-electron microscopy. Acta Crystallogr. D. ... Henderson, R. Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise. Proc. Natl Acad. Sci. USA ...
... thanks to high-contrast imaging in cryo-electron microscopy. Their study demonstrates Japans international competitiveness in ... Cryo-electron microscopy reveals shape of heterochromatin. Waseda University. Journal. Molecular Cell. Keywords. *BIOCHEMISTRY ... Cryo-electron microscopy reveals shape of heterochromatin Now that its structure has been defined, scientists are a step closer ... 2)Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna ...
The experimental technique of Cryo Electron Microscopy (Cryo-EM) complements those of X-Ray Crystallography and Nuclear ...
The method dubbed "cryo-electron microscopy" (cryo-EM) allows "high-resolution structure determination of biomolecules in ... Biochem boffins win the Nobel Prize for cryo-electron microscopy. Fancy method captures three-dimensional images of ...
... cryo-electron microscopy, cryo-EM, MBIB Division, microscopy, molecular biology, Molecular Biophysics and Integrated Bioimaging ... Researchers at Lawrence Berkeley National Laboratory and UC Berkeley have combined cutting-edge cryo-electron microscopy (cryo- ...
"Access to the National Cryo-Electron Microscopy Facility was originally published by the National Cancer Institute." ...
Cryo-electron microscopy of chromatin biology. Marcus D. Wilsona* and Alessandro Costaa* ... Owing to the nature of single-particle averaging in electron microscopy, an EM structure can span a large resolution range, ... Recent electron-microscopy (EM) studies on NCP-containing assemblies have helped to describe important chromatin transactions ... For example, early electron-microscopy (EM) work confirmed biochemical conclusions that the basic unit of chromatin is the ...
Cryo electron microscopy is booming, with new atomic structures appearing every week and new facilities being installed at ... Biophysics 101- Cryo-electron microscopy (Cryo-EM). 01:13:24. This video can only be viewed by current BPS members ... Cryo electron microscopy is booming, with new atomic structures appearing every week and new facilities being installed at ... Tags: Structural Biology cryo-EM Brandeis University Biophysics 101 Cryo electron microscopy atomic structures single-particle ...
Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise Message Subject (Your Name) has sent you ... 2013) De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. Elife ... Single particle cryo-electron microscopy is currently poised to produce high-resolution structures of many biological ... 2012) Four-dimensional cryo-electron microscopy at quasi atomic resolution: IMAGIC 4D. International Tables for Crystallography ...
Structure of a CLC chloride ion channel by cryo-electron microscopy.. Park E1, Campbell EB1, MacKinnon R1. ... Here we determined the structure of a bovine CLC channel (CLC-K) using cryo-electron microscopy. A conserved loop in the Cl- ...
Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution.. Osenkowski P1, Li H, Ye W, Li D, Aeschbach L ... Cryo-Electron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution ... Cryo-Electron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution ... Cryo-Electron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution ...
Cryo-electron microscopy (cryo-EM) extracts single-particle density projections of individual biomolecules. Although cryo-EM is ... In cryo-electron microscopy (cryo-EM) experiments a biomolecular sample is immersified in vitrified ice. The sample is then ... A Bayesian approach to extracting free-energy profiles from cryo-electron microscopy experiments. *Julian Giraldo-Barreto1,2, ... Cryo-electron microscopy (cryo-EM) extracts single-particle density projections of individual biomolecules. Although cryo-EM is ...
The program aims to broaden access to high-resolution cryoelectron microscopy (cryoEM) for biomedical researchers, by creating ... Transformative High Resolution Cryo-Electron Microscopy (CryoEM). *Transformative Research to Address Health Disparities and ... Transformative High Resolution Cryo-Electron Microscopy Program. The program is broadening access to high-resolution ... Did you miss one of the free monthly webinars on cryoEM methods hosted by the National Centers for Cryoelectron Microscopy? ...
Philips CM120 Cryo-Electron Microscope. Philips CM120 cryo-electron microscope is a computer-controlled transmission instrument ... Electron Microscopy Facility • 55 Lake Avenue North Worcester, Massachusetts 01655-0160 Questions or Comments? Email: gregory. ... dedicated to low dose and cryo-electron microscopic observations. Low electron dose images minimize specimen damage due to ...
News tagged with cryo electron microscopy. * Date 6 hours 12 hours 1 day 3 days all ...
... Insights allow researchers to control crystallization and could be ... Now, scientists have used cryo-electron microscopy (cryo-EM), the technique that took home the 2017 Nobel Prize in Chemistry, ...
... cryoelectron microscopy include Cryo-electron Microscopy Specimen Preparation By Means Of a Focused Ion Beam, Determination ... Dos and Donts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular ... Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction. ... Cryoelectron Microscopy: Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules ...
Volta phase plate cryo-electron microscopy structure of a calcitonin receptor-heterotrimeric Gs protein complex ... Here, we present the virion structures of DWV determined to a resolution of 3.1 Å using cryo-electron microscopy and 3.8 Å by X ... Structure of beta-galactosidase at 3.2-A resolution obtained by cryo-electron microscopy ... Cryo-Electron Microscopy (Cryo-EM) begins with vitrification, in which the protein solution is cooled so rapidly that water ...
Cryo-Electron Microscopy and the Complexity of Cancer. Updated about 1 year ago. ... Covering both biology and methodology, this webinar will explain how single-particle cryo-electron microscopy enables us to ...
Scientific Background: The development of cryo-electron microscopy. Pdf 837 Kb. To cite this section MLA style: Advanced ... The Nobel Prize in Physics 2017 - Scientific Background: The development of cryo-electron microscopy ...
Single-particle cryo-electron microscopy (cryo-EM) is an innovative technology for elucidating structures of biological ... Single-particle cryo-electron microscopy (cryo-EM) is an innovative technology for elucidating structures of biological ... Estimation in Extreme Noise Levels with Application to Cryo-Electron Microscopy Special Talk ... His current research is mainly focused on devising efficient computational tools for single particle reconstruction using cryo-electron ...
... electron tomography and microscopy of infected cells and of isolated virions. We find that PFV contains a nucleocapsid of ... Electron cryo-microscopy Is the Subject Area "Electron cryo-microscopy" applicable to this article? Yes. No. ...
Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly ... Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution subtomogram averaging. ... Determination of protein structure at 8.5Å resolution using cryo-electron tomography and sub-tomogram averaging ... Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging ...
Kristina Kermanshahche demos Cryo-Electron Microscopy for mapping protein structures on the Intel® Scalable System Framework at ... Cryo-Electron Microscopy (1:12) Jacquelyn Kottig demos using Intel® Xeon Phi™ processors and the ROME* system to visualize ... Advancing Cryo-Electron Microscopy for Life Sciences. Intel Life Sciences Global Director Kristina Kermanshahche demonstrates ... Cryo-Electron Microscopy for mapping protein structures and how the Intel® Scalable System Framework supports the required HPC ...
Cryo-electron microscopy (cryo-EM)-which enables the visualization of viruses, proteins, and other biological structures at the ... Cryo-Electron Microscopy Achieves Unprecedented Resolution Using New Computational Methods. Berkeley Lab researchers develop ... "This is a great example of how to exploit electron microscopy technology and combine it with new computational methods to ... of bacteriophage P22 generated with validated atomic models that were derived from a high-resolution cryo-electron microscopy ...
  • A national facility for biological cryo-electron microscopy. (ox.ac.uk)
  • Cryo-electron microscopy resolution continues to improve. (theconversation.com)
  • In the quest to find faster, better ways of mapping the structure of proteins and other key biological molecules, a growing number of researchers are turning to an innovative method that pushes the idea of a freeze frame to a whole new level: cryo-electron microscopy (cryo-EM). (nih.gov)
  • What is Cryo-Electron Microscopy (Cryo-EM)? (microscopes-online.info)
  • The laboratory dedicated to cryo-electron microscopy, where the equipment is located, will be fully accessible also to other research institutions and projects for the benefit of science and human health. (yesmilano.it)
  • introduction to crystallography + cryo-electron microscopy integration Confirmed speakers and tutors (so far. (phenix-online.org)
  • She and her team used a combination of two technologies-cryo-electron microscopy and X-ray crystallography-to see the virus and watch how it behaved. (newsweek.com)
  • As pharmaceutical labs turn to cryo-electron microscopy (cryo-EM) to uncover the structures of difficult-to-crystalize molecules at near atomic resolution, they need ways to increase their productivity to more quickly move from early drug discovery to clinical trials. (prnewswire.com)
  • This is an image of a structure of the human β3 GABAA receptor homopentamer solved to atomic resolution by cryo-electron microscopy (cryo-EM). (criver.com)
  • A system for storing and shipping samples for cryo-electron microscopy. (justia.com)
  • Expert on the development and use of cryo-electron microscopy (cryo-EM) as applied to viruses, bacteria, and human cells. (wisc.edu)
  • Learn about cryo-electron microscopy for whose development Prof. Frank received the 2017 Nobel Prize in Chemistry with Jacques Dubochet and Richard Henderson. (lindau-nobel.org)
  • The molecular basis of the disease is being decoded by the research group led by Professor Dieter Willbold, using extremely high-resolution structural biological methods such as NMR spectroscopy, X-ray crystallography and cryo-electron microscopy, as well as simulations run on Jülich's supercomputers. (fz-juelich.de)
  • Our favorite imaging technique is cryo-electron microscopy : we are using state-of-the art equipment available at the IBS EM platform and further afield to obtain images of our objects of interest. (ibs.fr)
  • Over the past ten years High-Performance Computing (HPC) has transformed medical research through advances in genomics, computational biology, cryo-electron microscopy, and numerous others forms of scanning, sequencing, and simulation. (cytel.com)
  • The postdoctoral position(s) will focus on developing and applying tools and methods for time-resolved crystallography, for cryogenic and time-resolved variable-temperature small-angle X-ray scattering, for single-particle cryo-electron microscopy, and for interpreting the resulting data to extract information about biomolecular structure, function, and energy landscapes. (academicjobsonline.org)
  • A special emphasis has been placed on setting up high-resolution cryo-electron microscopy (cryo-EM) methods, a powerful technique for high-resolution structural characterisation of individual molecules that is reshaping biomedical research. (cnio.es)
  • Finally we demonstrate, how dynamic performance tuning can be integrated into a real-world application from cryo-electron microscopy domain. (csic.es)
  • Our understanding of the static structure of the 80S eukaryotic ribosome has been enhanced by the emergence of high resolution cryo-electron microscopy and crystallography data over the past 15 years. (umd.edu)
  • The Cryo-EM facility at SLAC, built and operated in partnership with Stanford University, is equipped with multiple state-of-the-art instruments for cryo-electron microscopy, a groundbreaking technology that gives scientists unprecedented views of the molecular world. (stanford.edu)
  • Over the past several years, single-particle cryo-electron microscopy (cryo-EM) has emerged as a leading method for elucidating macromolecular structures at near-atomic resolution, rivaling even the established technique of X-ray crystallography. (sparrho.com)
  • Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography. (sparrho.com)
  • How Cryo-Electron Microscopy and X-ray Crystallography Complement Each Other. (sparrho.com)
  • We here report four structures of the trimeric CusA heavy-metal efflux pump in the presence of Cu(I) using single-particle cryo-electron microscopy (cryo-EM). (warwick.ac.uk)
  • Huntingtin protein's structure is now clear thanks to cryo-electron microscopy. (hdbuzz.net)
  • a number of the simplest methods include X-ray crystallography, cryo-electron microscopy and nuclear resonance aside from these methods there are many additional methods through which 3 D Structure Determination are often done. (expertconferences.org)
  • Cryo-electron microscopy (cryo-EM) is a powerful technique used to solve the 3D structures of proteins and other biomolecules. (nature.com)
  • Here, we applied virtual nanoscopy in a correlative light-electron microscopy study to address the role of the endothelial glycocalyx in protein leakage over the glomerular filtration barrier, in an immunogold labeling study of internalization of oncolytic reovirus in human dendritic cells, in a cryo-electron microscopy study of intact vitrified mouse embryonic cells, and in an ultrastructural mapping of a complete zebrafish embryo slice. (rupress.org)
  • Despite the long history of structure-mechanism studies using soluble receptor domains or intact yet isolated receptors, structures of AMPA receptor-auxiliary subunit complexes have not been available until recent breakthroughs in single-particle cryo-electron microscopy. (elsevier.com)
  • We then use our defined modified chromatin to study individual nucleosome-chromatin protein complexes using single-particle cryo-electron microscopy ( cryo-EM ), Biochemical, Biophysical and Cell Biology approaches to investigate histone marks and DNA methylation. (mdwilsonlab.com)
  • Cryo-electron microscopy of chromatin biology. (mdwilsonlab.com)
  • The cryo-electron microscopy structure of huntingtin. (pku.edu.cn)
  • Are you about to start designing your first cryo-electron microscopy (cryo-EM) experiment, or are you a seasoned cryo-EM pro looking for the latest news and advancements in life science research using cryo-EM? (labroots.com)
  • Date: April 29, 2021 Time: 9:00am PST Cryo-electron microscopy (cryo-EM) reached single-atom resolution for 3D structure determination of biological macromolecules. (labroots.com)
  • Cryo-electron microscopy turned this on its head. (collegetribune.ie)
  • Preparation of macromolecular complexes for cryo-electron microscopy. (scienceservices.de)
  • Using cryo-electron microscopy, the researchers uncover key structures, including a large coiled region and a small, flexible claw. (mit.edu)
  • To achieve that view, Rogala turned to a method known as cryo-electron microscopy or cryo-EM. (mit.edu)
  • Cryo-electron microscopy (cryo-EM) represents the next front. (acceleratingscience.com)
  • Figure 1: The structure of carboxysomes and the Rubisco octamers occupying them as determined using cryo electron microscopy. (bionumbers.org)
  • He uses cryo-electron microscopy (cryoEM) to visualize these molecules at near-atomic resolution as they are being assembled and changing shape while they work. (mit.edu)
  • In our research group we are using a combination of in vivo assays, biochemistry and cryo-electron microscopy to study macromolecular complexes of specialized pathogenic organisms. (umu.se)
  • Postdoctoral and PhD positions are available for researchers who would like to apply state-of-the-art techniques in cryo-electron microscopy to study important processes in pathogenic organisms. (umu.se)
  • Interested in doing a master thesis in cryo-electron microscopy? (umu.se)
  • MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. (cool-temp.co.za)
  • The structures were solved independently by x--ray crystallography and cryo--electron microscopy. (nysbc.org)
  • The work includes all aspects of molecular and structural biology including cryo-electron microscopy, cloning, protein expression, and protein biochemistry. (cbia.org)
  • The ability to learn new skills related to all aspects of cryo-electron microscopy. (cbia.org)
  • Cryo-electron microscopy - CryoEM image of GroEL suspended in vitreous ice at 50,000X magnification. (academic.ru)
  • We are also supplying our structural biologists, led by Christiane Schaffitzel, with mutant and variant forms of the viral proteins for cryo-electron microscopy. (rsb.org.uk)
  • Cryo-electron microscopy (cryo-EM) reconstruction at subnanometer resolution revealed a ~90° hinge rotation accompanying NLRC4 activation. (cdc.gov)
  • Using cryo-electron microscopy, we now visualize the functional maedi-visna lentivirus intasome at 4.9 angstrom resolution. (diamond.ac.uk)
  • Relion 3.1 (released July 2020) is an image processing software designed specifically for cryo-electron microscopy (cryo-EM). (linuxvixion.com)
  • Three-dimensional electron microscopy is an enormously powerful tool for structural biologists. (ox.ac.uk)
  • Here, a brief overview is provided of the plans for a UK national three-dimensional electron-microscopy facility for integrated structural biology to enable internationally leading research on the machinery of life. (ox.ac.uk)
  • Structural insight into transmissive mutant huntingtin species by correlative light and electron microscopy and cryo-electron tomography. (pubfacts.com)
  • Using electron microscopy and high-speed atomic force microscopy, researchers show the internal molecular motor behind the gliding mechanism for Mycoplasma mobile to consist of two ATP synthase-like molecules. (asiaresearchnews.com)
  • A whole cell image (left), motor images reconstructed from electron microscopy (middle), and a motor schematic (right) are shown. (asiaresearchnews.com)
  • In collaboration with Osaka University and Kanazawa University, his research team used electron microscopy and high-speed atomic force microscopy (high-speed AFM) to reveal that the bacteria's molecular motor consists of two ATP synthase-like complexes, suggesting an unexpected evolution of the protein. (asiaresearchnews.com)
  • Using negative-staining electron microscopy, they discovered a twin motor where each motor is structurally similar to ATP synthase. (asiaresearchnews.com)
  • Our approach employs standard transmission electron microscopy, rapid automated data collection, and stitching to create large virtual slides. (rupress.org)
  • It greatly facilitates correlative light-electron microscopy studies to relate structure and function and provides a genuine representation of ultrastructural events. (rupress.org)
  • Jacques Dubochet came along shortly after the two lads and added water to electron microscopy. (collegetribune.ie)
  • Spores were resuspended in electron microscopy (EM) buffer (30 mM Tris-HCl (pH 7. (eimearbyrnedance.com)
  • EMAN2: an extensible image processing suite for electron microscopy. (thecoinradar.com)
  • Assist with electron microscopy grid preparation and data collection. (cbia.org)
  • Что такое Analytical Electron Microscopy? (academic.ru)
  • Photoemission electron microscopy - (PEEM, also called photoelectron microscopy, PEM) is a widely used type of emission microscopy. (academic.ru)
  • Aberration-Corrected Analytical Transmission Electron Microscopy , Rik Brydson. (academic.ru)
  • Deep learning assisted transmission electron microscopy. (emc2020.eu)
  • Scipion is an image processing framework to obtain 3D models of macromolecular complexes using Electron Microscopy. (linuxvixion.com)
  • The European Microscopy Congress 2020 is being hosted by SCANDEM, and organised by the UK's Royal Microscopical Society. (emc2020.eu)
  • We solubilized and isolated unliganded and CD4-bound spikes from virus-like particles and used cryoelectron microscopy to reconstruct their 3D structures. (ncku.edu.tw)
  • Field emission microscopy - (FEM) is an analytical technique used in materials science to investigate molecular surface structures and their electronic properties. (academic.ru)
  • Photoconductive atomic force microscopy - (pc AFM) is a scientific technique. (academic.ru)
  • The group of Prof. Warren Zipfel at Cornell University develops and applies novel optical microscopy methods for biomedical research and clinical imaging. (hercjobs.org)
  • The next Scripps Research Front Row Lecture at 1 p.m. Wednesday, June 17, will be a virtual event featuring structural biologist Andrew Ward speaking on how his lab is using a revolutionary technique known as cryoelectron microscopy to understand the precise structure of the root virus that causes COVID-19. (ranchosantafereview.com)
  • Structural basis for the function of a small GTPase RsgA on the 30S ribosomal subunit maturation revealed by cryoelectron microscopy. (pku.edu.cn)
  • Microscopy - is the technical field of using microscopes to view samples and objects that cannot be seen with the unaided eye (objects that are not within the resolution range of the normal eye). (academic.ru)
  • High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer. (cornell.edu)