Cryoelectron Microscopy
Cryoultramicrotomy
Microscopy, Electron
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, Molecular
Atadenovirus
Negative Staining
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.
Image Processing, Computer-Assisted
Protein Conformation
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).
Models, Structural
Electron Microscope Tomography
Encephalomyelitis, Western Equine
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)
Virion
Protein Structure, Quaternary
Crystallography, X-Ray
Tomography
Virus Assembly
Microscopy
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.
Rhinovirus
Crystallization
Protein Structure, Tertiary
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.
Imaging, Three-Dimensional
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.
X-Ray Diffraction
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)
Cryopreservation
Immunoglobulin Fab Fragments
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.
Binding Sites
Microscopy, Electron, Scanning
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.
Molecular Sequence Data
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.
Protein Structure, Secondary
Amino Acid Sequence
Macromolecular Substances
Microscopy, Confocal
Receptors, Virus
Protein Subunits
Dimerization
Protein Binding
Microscopy, Fluorescence
Endoplasmic Reticulum, Rough
Sequence Homology, Amino Acid
Escherichia coli
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.
Microscopy, Atomic Force
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.
Microscopy, Electron, Transmission
Microscopy, Immunoelectron
Sindbis Virus
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)
ASTM E3143 - 18b Standard Practice for Performing Cryo-Transmission Electron Microscopy of Liposomes
Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies<...
ASSISTANT PROFESSOR IN CRYO ELECTRON MICROSCOPY job with University of California, Irvine | 417876
Single-Particle Cryo-EM of Membrane Proteins in Lipid Nanodiscs | SpringerLink
Improved methods for single-particle cryogenic electron microscopy
Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo-electron microscopy | Research -...
Structural markers in prostate cancer serum imaged ex vivo using cryogenic transmission electron microscopy
Resolving the Morphology of Peptoid Vesicles at the 1 nm Length Scale Using Cryogenic Electron Microscopy.
Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography<...
RCSB PDB - 3JBP: Cryo-electron microscopy reconstruction of the Plasmodium falciparum 80S ribosome bound to E-tRNA
Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. - Nuffield Department of Medicine
The resolution revolution continues: GIF Quantum LS imaging filter with K2 Summit camera enables scientists to reach 2.2 Ã…...
Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome.
Using molecular approaches to understand Complex I deficiency in mouse models
High resolution single-particle cryo-EM of a 200 kDa membrane ion channel | NIH Research Festival
Cryo Electron Microscopy Short Course 2010 | IPRIME
Solubilization of nonionic monoalkyl amphiphile-cholesterol vesicles by octyl glucoside: Cryo-transmission electron microscopy...
High resolution cryo-electron microscopy of clathrin cage networks at University of Warwick on FindAPhD.com
Cryo-EM structure of oxysterol-bound human Smoothened coupled to a heterotrimeric G<sub>i</sub> ...
Localization of eukaryote-specific ribosomal proteins in a 5.5-Ã… cryo-EM map of the 80S eukaryotic ribosome<...
ccp4bb] EMBO practical course on image processing for cryo-electron microscopy
single-particle electron cryomicroscopy Archives | The Emory Wheel
Cryo electron microscopy of membrane proteins and biomolecular assemblies - Hans Hebert | Department of Biosciences and...
CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations. - Nuffield Department of...
Single particle analysis - Wikipedia
Single-particle cryo-EM of the ryanodine receptor from skeletal muscle by Alex H. Will
A Bayesian adaptive basis algorithm for single particle reconstruction. - PubMed - NCBI
Events - Instruct-ERIC
Stringent Response: Tet(O) cryoEM structure is out!
PDB-6id0: Cryo-EM structure of a human intron lariat spliceosome prior to P... - Yorodumi
PDB-5n5n: Cryo-EM structure of tsA201 cell alpha1B and betaI and betaIVb mi... - Yorodumi
News : EMDataResource
How smart, ultrathin nanosheets go fishing for proteins | Max Planck Institute of Biophysics
Spectroscopy Society of Pittsburgh » February Monthly Meeting
Forschungszentrum Jülich - Ansprechpartner - Prof. Dr. Carsten Sachse
Electron cryomicroscopy shows cardiac thin filament structure -- MEDICA - World Forum for Medicine
APPROACHING VIRUS LIFE CYCLE WITH ELECTRON MICROSCOPY | IMRI
Cryoelectron Microscopy of Icosahedral Virus Particles | SpringerLink
Zinc in the structure of Drosophila Nod (3DC4) and Bovine Tubulin (1JFF) Docked Into The 11-Angstrom Cryo-Em Map of Nucleotide...
Publications
New indication of a link between Alzheimers and diabetes | EurekAlert! Science News
Scientists take cool look at dendrite growth - Materials Today
Mapping the Structure and Function of the E1 and E2 Glycoproteins in Alphaviruses - CaltechAUTHORS
Cryo-electron microscopy of viruses | Gelbart Lab
First appointment in new Salk Fellows Program - Salk Institute for Biological Studies
Cryo-EM structure of a licensed DNA replication origin | Crick
Worlds leading supplier of electron microscopy solutions partners with Imaging CoE for R&D - Imaging CoE
Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics - Fingerprint
- University of...
Phasing of the Triatoma virus diffraction data using a cryo-electron microscopy reconstruction. - Institut Pasteur
Cryo Electron Microscopy and Electron Tomography - Drug Discovery World (DDW)
Cryo-electron tomography of cells: connecting structure and function :: MPG.PuRe
Combined Cryogenic Transmission Electron Microscopy and Electron Spin Resonance Studies of Egg Phosphatidylchloline Liposomes...
Cryo-electron Microscopy Structure of the Native Prototype Foamy Virus Glycoprotein and Virus Architecture - Université...
Cryo Electron Microscopy scoops Nobel Prize in Chemistry. | Department of Political Studies
Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus
Delmic Microscopy Blog | cryo-electron tomography
Rapid tilt-series method for cryo-electron tomography: Characterizing stage behavior during FISE acquisition - CaltechAUTHORS
Simulating cryo electron tomograms of crowded cell cytoplasm for assessment of automated particle picking | BMC Bioinformatics ...
Joachim Frank Wins Nobel Prize in Chemistry
Structural studies of human immunodeficiency virus type 1 by cryo-electron tomography - CaltechTHESIS
Bsoft: References
Electron Crystallography of Soluble and Membrane Proteins - beck-shop.de
Cryoelectron tomography - Latest research and news | Nature
Structure of the full-length HCV IRES in solution
Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. | MRC Mitochondrial Biology Unit
Protein structure could unlock new treatments for cystic fibrosis - Scienmag: Latest Science and Health News
Capsids of tricorn protease studied by electron cryomicroscopy :: MPG.PuRe
Coacervation of Elastin-Like Recombinamer Microgels
Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome. « RNomics
Soft cellulose II nanospheres: sol gel behaviour, swelling and material synthesisBeaumont, Marco; Rosenfeldt, Sabine; Tardy,...
Project abstract for group mccormic | Minnesota Supercomputing Institute
Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo - Oxford Particle...
Ariane Briegel - Leiden University
Cryo-EM reconstruction of the giant Mimivirus using C5 symmetry | NIH 3D Print Exchange
Viruses | Free Full-Text | Fluorescent Protein-Tagged Sindbis Virus E2 Glycoprotein Allows Single Particle Analysis of Virus...
Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase. | MRC Mitochondrial Biology Unit
First atomic model of human telomerase constructed by electron cryo-microscopy
Dirksen E. Bussiere | ACS Division of Biological Chemistry Website
The Stephen Long Lab: Publications | Sloan Kettering Institute
Freezing immunoglobulins to see them move
Virus caught in the act of infecting a cell
Spatial Localization of the Ebola Virus Glycoprotein Mucin-Like Domain Determined by Cryo-Electron Tomography
HIV-1 Biogenesis Studied by Cellular Cryo-Electron Tomography and Biochemical in vitro Reconstitution - ORA - Oxford University...
Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations -...
Glycoprotein Ib clustering in platelets can be inhibited by α-linolenic acid as revealed by cryo-electron tomography |...
Conveyor technology: Non-Contact Optical Vibration Measurement with Subnanometer Resolution
Multivariate Statistical Analysis of Large Datasets: Single Particle Electron Microscopy
Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding.
Magnetic imaging with a Zernike-type phase plate in a transmission electron microscope
Undergraduate | Stanford EE
Ribosome and ribosomal RNA Structure : An experimental and computational analysis of expansion segments in eukaryotic ribosomal...
Difference between revisions of Colloquia - Math
Difference between revisions of Colloquia - Math
No data available that match "cryoelectron microscopy"
Cryoelectron Microscopy of Vitrified Specimens | SpringerLink
... 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 ...
Cryo-electron microscopy | imaging technique | Britannica.com
... 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 | KTH
Cryoelectron Microscopy of Icosahedral Virus Particles | SpringerLink
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 ...
Real-time cryo-electron microscopy data preprocessing with Warp | Nature Methods
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 ...
Cryo-electron microscopy reveals shape of heterochromatin | EurekAlert! Science News
... 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 ...
Ryan H Lilien - Project Profile: Cryo-Electron Microscopy
Biochem boffins win the Nobel Prize for cryo-electron microscopy • The Register
cryo-electron microscopy
Access National Cryo-Electron Microscopy Facility - National Cancer Institute
IUCr) Cryo-electron microscopy of chromatin biology
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 ...
Biophysics 101- Cryo-electron microscopy (Cryo-EM)
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 | PNAS
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. - PubMed - NCBI
Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution. - PubMed - NCBI
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 ...
A Bayesian approach to extracting free-energy profiles from cryo-electron microscopy experiments | Scientific Reports
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 ...
Transformative High Resolution Cryo-Electron Microscopy (CryoEM)
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 Core Electron Microscopy Facility - UMASS Medical School
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 ...
Phys.org - cryo electron microscopy
Cryo-electron microscopy reveals how protein crystals grow
'cryoelectron microscopy' Protocols and Video...
... 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 ...
The History of Cryo-Electron Microscopy | Thermo Fisher Scientific
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 Ã… using cryo-electron microscopy and 3.8 Ã… 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 | Hipcast
The Nobel Prize in Physics 2017 - Scientific Background: The development of cryo-electron microscopy
Estimation in Extreme Noise Levels with Application to Cryo-Electron Microscopy | Duke Computer Science
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 ...
Cryo-electron Microscopy Structure of the Native Prototype Foamy Virus Glycoprotein and Virus Architecture
Cryo-Electron Microscopy Service Platform - Members - EMBL
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 8.5Ã… 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 ...
Advancing Cryo-Electron Microscopy for Life Sciences
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 Achieves Unprecedented Resolution Using New Computational Methods | Berkeley Lab
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 ...
Cryo-electron m53
- 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)
Electron microscopy18
- 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)
20201
- The European Microscopy Congress 2020 is being hosted by SCANDEM, and organised by the UK's Royal Microscopical Society. (emc2020.eu)
Structures2
- 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)
Atomic1
- Photoconductive atomic force microscopy - (pc AFM) is a scientific technique. (academic.ru)
Prof1
- The group of Prof. Warren Zipfel at Cornell University develops and applies novel optical microscopy methods for biomedical research and clinical imaging. (hercjobs.org)
Structural2
- 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)
Resolution2
- 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)