Creative Biostructure, an expert in the supplying of products and services for structural biology studies, recently built X-ray Crystallography Platform to provide support to customers from both industry and academia for their structural biology projects.. Scientists in this field can have access to Creative Biostructures state-of-the-art tools and identify and optimize crystallization conditions as well as X-ray diffraction data processing for any macromolecule of interest.. X-ray crystallography is one of the most favored techniques for the determination of the atomic structure of proteins, nucleic acids and other molecules. This platform in Creative Biostructure is equipped with highly specialized instruments for X-ray diffraction studies, including multipurpose diffractometers, nano-liter crystallization robots, high-throughput liquid handling robots and high-resolution imaging systems. With advanced equipment and experienced crystallographers, the company is able to set up crystallization ...
Written by Tatjana Barthel Macromolecular Crystallography group at BESSY II). The outbreak of SARS-CoV-2 pushed all of us into a very complicated situation, especially with strict regulations and certain lockdown periods. Performing science became challenging in these last weeks, but at the same time it is of great importance in order to fight the virus. In the development of drugs against SARS-CoV-2 X-ray crystallography plays a key role.. One field of X-ray crystallography is protein crystallography. Proteins can form crystals just as small molecules, metals and salts. The array of ordered protein molecules inside a protein crystal leaves gaps that are filled by disordered solvent molecules, i.e. mostly water. These so called solvent channels enable small molecules to enter the protein crystals and reach the individual protein molecules. Thus, protein crystals can be used for drug development, by probing them with small molecules in order to find out if and how the molecules bind to the ...
We use X-ray diffraction data provided by diffractometers and/or synchrotron sources to study protein samples using X-ray Crystallography methods:. Mechanistic studies and identification of ligands, at atomic level We have a strong, internationally recognized, expertise in the structural studies of enzymes, like nitrate reductases and aldehyde oxidases from different organisms, and X-ray crystallography methods have helped clarifying the details of several enzymatic mechanisms Drug design and ligand discovery We use several blood plasma proteins to study the recognition (at atomic level) and/or transport of candidate drugs to treat many diseases. Crystallography data has allowed to view the protein-drug interactions, at an atomic level Glycan-protein and protein-protein interactions We have used X-ray crystallography, associated to other biophysical methods, to study big molecular assemblies that function like nanomachines. X-ray diffraction, cryo-EM and SAXS data have been crucial to ...
X-ray crystallography is a technique used by biochemist to determine the three dimensional structure of an enzyme, protein, molecule, etc. Although the technique requires the molecule to be able to be crystallized it has helped scientist discover how drugs can prevent certain enzyme from reacting. By determining the three dimensional structure of the protein or enzyme scientists can determine how enzyme folds and binds. From that information, scientists can design certain drugs that only stop that enzyme. For example, scientists used x-ray crystallography to determine the structure of the COX enzyme that is responsible for arthritis. Now that the scientists know the three dimensional structure of the COX enzyme, they can create drugs that would be able to stop it, such as aspirin. Therefore X-ray crystallography is a powerful tool that biochemist and scientists can use to discover new drugs that can prevent certain enzymes from activating.. ...
Post-doctoral Positions in X-ray Crystallography and Computational Biology Two post-doctoral positions are available immediately, one in experimental and one in computational aspects of protein crystallography. Applicants for the first position should be experienced in practical aspects of protein crystallography and structure determination. Experience in cloning and protein expression is also desirable. Crystals are already in hand for one novel carotenoid-binding protein. Subsequent projects will diversify to include work on self-assembling proteins and other proteins with repetitive or otherwise unusual architectures. The second position is in the area of computational crystallography, but may also include other aspects of computational biology such as genomics or protein structure analysis. The successful applicant should have a strong background in scientific programming, an understanding of numerical methods, and an ability to solve complex problem. Familiarity with crystallographic and ...
The International Union of Crystallography is a non-profit scientific union serving the world-wide interests of crystallographers and other scientists employing crystallographic methods ...
I just finished reading your oped article on reproducibility in science. As an experimental scientist - more precisely a chemical crystallographer - I have had to deal with this kind of situation a number of times, and at least two examples may serve as the possible exceptions to your rules.. One of the beauties of x-ray crystallography is the internal self-consistent confirmation of the result of an x-ray crystal structure determination. X-ray crystal structure determinations are today used (increasing required by journals) as essentially absolute proof of the molecular structure of a new compound. With the result of a determination there is no doubt that the crystal from which the data were obtained contained molecules with the composition and structure that can be represented by a three dimensional ball and stick model. There occasionally are some problems with measurements and refinements of structures, but they are a very, very small fraction of the mass of crystal structures (now nearing ...
where Nall is the total number of atoms and Npeak is the number of atoms which contain one or more peaks within 2.2 Å of the atom.. In order to analyse the effect of X-ray resolution, m,Fo, − D,Fc, electron-density maps were generated at five different resolutions as follows. The same X-ray refinements as those in the above procedure were performed for DNA crystal structures solved at a resolution equal to or better than 2.5 Å. The m,Fo, − D,Fc, map was calculated at 1.0, 1.25, 1.5, 1.9 and 2.5 Å resolution for data of ≤1.0, 1.0-1.25, 1.25-1.5, 1.5-1.9 and 1.9-2.5 Å resolution, respectively. A search was made for peaks in the maps in the same way as above.. In this study, the r.m.s. of densities (σ) was used to distinguish peaks from noise. The density of electrons (e Å−3) can also be used and this different measure might give a different result. We then investigated the variation of electron density corresponding to 1σ in the electron-density maps. Supplementary Fig. S2 shows the ...
X-ray crystallography is the major method for structure determination of macromolecules. About 85% of all known structures deposited in the Protein Data Bank have been determined by X-ray crystallography. Knowing the structure of a protein helps in understanding better how the protein works, how it interacts with other proteins and small molecules in the cell and what kind of conformational changes it undergoes to exert its function. Even subtle changes in protein structures can have tremendous consequences on human health, causing serious diseases. A major application therefore of X-ray crystallography is in the design of new drugs.. A crystal structure determination is not a trivial task. It mainly involves five steps with the first two being the most difficult (bottlenecks):. ...
1GNR: X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp.
ABSTRACT. High-throughput crystallography requires a method by which the structures of proteins can be determined quickly and easily. Experimental phasing is an essential technique in determining the three-dimensional protein structures using single-crystal X-ray diffraction. In macromolecular crystallography, the phases are derived either by Molecular Replacement (MR) method using the atomic coordinates of a structurally similar protein or by locating the positions of heavy atoms that are intrinsic to the protein or that have been added (MIR, MIRAS, SIR, SIRAS, MAD and SAD). Availability of in-house lab data collection sources (Cu Kα and Cr Kα radiation), cryo-crystallography and improved software for heavy atom location and density modification have increased the ability to solve protein structures using SAD. SAD phasing using intrinsic anomalous scatterers like sulfur, chlorine, calcium, manganese and zinc, which are already present in the protein becomes increasingly attractive owing to ...
The -ray crystal-structure analysis of 1,3-diadamantylaziridinone (1b) demonstrates that the configuration at nitrogen is pyramidal (N lying 0·534 Å from the plane defined by its three substituents) and that the adamantyl groups are to each other.
The Crystallography Times newsletter from Rigaku Oxford Diffraction focuses on single crystal X-ray diffraction and is available from the companys website October 30, 2017 - The Woodlands, Texas. The latest edition of Crystallography Times, the X-ray crystallography newsletter from Rigaku Oxford Diffraction, is now available to view on the companys global website. 1600181092
Two user-friendly computer programs are described for use in macromolecular X-ray crystallography, xdlMAPMAN provides an interface for electron-density map exchange between some of the most commonly used phase refinement, structure refinement and model- building programs. In addition, it contains several options to analyse and abstract such maps. xdlDATAMAN provides similar functionality for the analysis and manipulation of macromolecular reflection data sets. Both programs have a simple graphical user interface, and their source code has been put into the public domain.. ...
The Woodlands, Texas (PRWEB) August 30, 2017 -- The latest edition of Crystallography Times, the X-ray crystallography newsletter from Rigaku Oxford
Creative Biolabs offers high-throughput X-ray crystallography or Protein crystallography services for protein-protein interaction assays.
The conjugative transfer of F-like plasmids is repressed by FinO, an RNAbinding protein. FinO interacts with the F-plasmid encoded traJ mRNA andits antisense RNA, FinP, stabilizing FinP against endonucleolyticdegradation and facilitating sense-antisense RNA recognition. Here wepresent the 2.0 A resolution X-ray crystal structure of FinO, lacking itsflexible N-terminal extension. FinO adopts a novel, elongated, largelyhelical conformation. An N-terminal region, previously shown to contactRNA, forms a positively charged alpha-helix (helix 1) that protrudes 45 Afrom the central core of FinO. A C-terminal region of FinO that isimplicated in RNA interactions also extends out from the central body ofthe protein, adopting a helical conformation and packing against the baseof the N-terminal helix. A highly positively charged patch on the surfaceof the FinO core may present another RNA binding surface. The results ofan in vitro RNA duplexing assay demonstrate that the flexible N-terminalregion of FinO ...
Yu, L. (Creator), Dong, X. (Creator), Gong, Q. (Creator), Acharya, S. R. (Creator), Lin, Y. (Creator), Wang, H. (Creator), Han, Y. (Creator), Thonhauser, T. (Creator), Li, J. (Creator), Yu, L. (Creator), Gong, Q. (Creator), Acharya, S. R. (Creator), Lin, Y. (Creator), Wang, H. (Creator), Thonhauser, T. (Creator), Li, J. (Creator) (Apr 7 2020). CCDC 1970606: Experimental Crystal Structure Determination : catena-[bis(mu-4,4,4-[benzene-1,3,5-triyltris(oxy)]tribenzoato)-tris(mu-hydroxy)-tri-aluminium(iii) 3-methylpentane unknown solvate]. Cambridge Crystallographic Data Centre. 10.5517/ccdc.csd.cc244kyt ...
Up to four post-doctoral positions are available immediately in the new laboratory of Dr. Bob Liddington at the Burnham Institute, La Jolla, California, to work on the structural biology of membrane proteins, including integrins, ion channels and toxins. Both experienced crystallographers and protein chemists are sought. The Burnham Institute is adjacent to Scripps, the Salk Institute, the UCSD campus and the Pacific Ocean. Daytime highs currently around 70 F (21 C) with unbroken blue skies. Reply to rlidding at burnham-inst.org ...
This motorized stage allows for rapid switching between alignments optimized for electronic absorption and for Raman spectroscopy. Reproducibility of the stage position was determined by the manufacturer (CrystalLogic, CA, USA) to be within 2.5 µm in each of x, y and z. The SuperHead collects both Rayleigh and Raman scattered light in a backscatter (180°) mode. An edge filter within the SuperHead removes the Rayleigh scatter. The Raman scattered light is focused into another 100 µm fiber optic which connects to an iHR320 spectrometer (Horiba Jobin-Yvon). The entrance slit width is adjustable with a maximal width of 2 mm. Three gratings on a motorized turret are available: 600, 1200 and 1800 lines mm−1. The user can easily switch between the collection of broad low-resolution spectra and the collection of high-resolution spectra from a narrow region of particular interest. The detector is a Peltier-cooled (203 K) Synapse CCD detector (Horiba Jobin-Yvon). The CCD chip is a front-illuminated ...
Why this is my favorite X-ray crystal structure: The beautiful, strikingly unique structure of B-rhombohedral boron has successfully withstood numerous challenges of its correctness and has for a half century experienced nearly constant investigations of its structurally implied material characteristics. Arguably the most important of the several known phases of elemental boron, this form has been found to be experimentally stable from absolute zero to its melting point. Detailed consideration of the 5-foldness of its numerous discrete and merged 12-atom regular icosahedral motifs and their extended 84-atom truncated icosahedral arrays has forced a significant modification of chemical bonding theory in attempts to explain the low density, high strength, high melting, semiconducting and other notable properties of this low atomic number element. Even the observed partial occupancy of one of its 6-fold Wyckoff sets of atoms within the structure appears to be correct and to imply intriguing ...
CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Phaser is a program for phasing macromolecular crystal structures by both molecular replacement and experimental phasing methods. The novel phasing algorithms implemented in Phaser have been developed using maximum likelihood and multivariate statistics. For molecular replacement, the new algorithms have proved to be significantly better than traditional methods in discriminating correct solutions from noise, and for single-wavelength anomalous dispersion experimental phasing, the new algorithms, which account for correlations between F + and F, give better phases (lower mean phase error with respect to the phases given by the refined structure) than those that use mean F and anomalous differences F. One of the design concepts of Phaser was that it be capable of a high degree of automation. To this end, Phaser (written in C++) can be called directly from Python, although it can also be called using traditional CCP4 keyword
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Sodium atom in PDB 1uy1: Binding Sub-Site Dissection of A Family 6 Carbohydrate-Binding Module By X-Ray Crystallography and Isothermal Titration Calorimetry
Figure 1 - Scientists supported in attending the Erice school through CCDC travel bursaries - Abishek Chitnis from Mumbai University (left) and Madan Kumar from Mangalore University (right). Abishek is working in the field of high pressure physics, in particular looking at the stability of perovskite metal-organic frameworks. He commented that during the Erice School he got to know about different research areas, ideas & opportunities in high pressure crystallography as well as enjoying healthy conversations and discussion with lecturers and experts. Abishek also commented that I learnt many things as well as enjoyed this school. I am very grateful to the organizers and volunteers for the arrangements and all kind of comforts and supports we obtained.. Madan Kumar is based at the PURSE lab at Mangalore University. He has worked with both small molecule crystallography as well as the structure determination of proteins from single crystal x-ray diffraction. Madan commented that the hands-on ...
The workshop will include comprehensive theoretical lectures on all facets of crystallographic structure determination and hands-on tutorials. The lectures will be open to all, but the tutorials will be limited to 20 participants that will be chosen by committee. Lectures and tutorials will be given by Tom Terwilliger (Los Alamos), Randy Read (Cambridge), Zbigniew Dauter (Argonne), Karine Sparta (from the XDS development group) and members of the TCSB. The cost of participation in the full program is 200 Euro. More information, including fellowships, and the registration page can be found: http://tcsb-biox-wksp.net.technion.ac.il.. ...
This paper introduces ISOLDE, a new software package designed to provide an intuitive environment for high-fidelity interactive remodelling/refinement of macromolecular models into electron-density maps. ISOLDE combines interactive molecular-dynamics flexible fitting with modern molecular-graphics v …
We analyze small molecule ligand binding to ATAD2 bromodomain by molecular dynamics and protein crystallography. We observe a previously unexplored conformation of the binding pocket upon rearrangement of the gatekeeper residue Ile1074. Minor differences in the ligands result in binding with different plasticity of the ZA loop.. Visit the publication. ...
The Alber lab at UC Berkeley is pleased to release of the code for Ringer version 1.0 (http://ucxray.berkeley.edu/ringer.htm), which depends on Chimera. Ringer is a program to detect molecular motions by systematic X-ray electron-density sampling. The aim of Ringer is to go beyond static structural snapshots of proteins by uncovering structural ensembles in X-ray electron density. This information can reveal not only which parts of proteins are flexible and which parts are rigid, but it also can define alternate conformations that may be important for function. Alternate conformations of binding sites also may afford additional targets for drug design. The Ringer method is described in Lang et al. /Protein Sci/. 2010 Jul; 19(7):1420-31 ,http://www.ncbi.nlm.nih.gov/pubmed/20499387,. An application of Ringer, determining the structural underpinnings of the side chain dynamics critical for the function of the enzyme proline isomerase, was published in Fraser JS et al. /Nature/. 2009 Dec ...
The Protein crystallography core facility of Biocenter Oulu has the infrastructure for protein structural studies from crystallization to x-ray data collection and structure determination.
TY - JOUR. T1 - X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC). AU - Domingo Meza-Aguilar, J.. AU - Fromme, Petra. AU - Torres-Larios, Alfredo. AU - Mendoza-Hernández, Guillermo. AU - Hernandez-Chiñas, Ulises. AU - Arreguin-Espinosa De Los Monteros, Roberto A.. AU - Eslava Campos, Carlos A.. AU - Fromme, Raimund. PY - 2014/3/7. Y1 - 2014/3/7. N2 - Autotransporters (ATs) represent a superfamily of proteins produced by a variety of pathogenic bacteria, which include the pathogenic groups of Escherichia coli (E. coli) associated with gastrointestinal and urinary tract infections. We present the first X-ray structure of the passenger domain from the Plasmid-encoded toxin (Pet) a 100 kDa protein at 2.3 Å resolution which is a cause of acute diarrhea in both developing and industrialized countries. Pet is a cytoskeleton-altering toxin that induces loss of actin stress fibers. While Pet (pdb ...
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.
The Chemical Crystallography Service is run in two parts: the analytical service and the DIY service which includes some 40 trained users. It is a special feature of the X-ray crystallography laboratory in Oxford that hands-on crystallography is promoted. Initially researchers who want to determine their own structures complete a minimal practical health and safety course and are invited to attend crash-courses on crystal structure analysis. Following tailored one-to-one training in the use of the instrumentation, structure solution/refinement software, preparing files for publication and validation, data can be collected unsupervised, although help is always available in case of difficulties. Some examples of structures published by The Service are shown left.. In addition to the in-house instrumentation, we also have regular access to the Small Molecule Beamline at the Diamond Light Source, I19 (bottom left) under the Block Allocation System. As part of The Service, trained users have ...
Water is one of the simplest molecule on earth and essential to life. Well known molecule, it is in the same time a molecule that still not completely known when grouped with other water molecule. Snowflakes show broad number of structures, from which mechanical behavior will depend. Macroscopic mechanical behavior of snow, especially in montains, depends then only of the weak very small hydrogen bonds. In the same time not so weak as USA think to use it with wood fibers to build armor for warships as strong as metallic ones during the WWII. -Pennarun. ...
The 220 kDa dimeric cytochrome b6f complex of oxygenic photosynthesis provides the electronic connection between the two reaction centers, Photosystems I and II that are, respectively, coupled to NADP+ reduction and oxygen evolution. The electron transport functions of the b6f complex are coupled to proton transfer and generation of a trans-membrane proton electrochemical gradient, by mechanisms similar to those of the cytochrome bc1 complex of the respiratory chain and the photosynthetic bacteria, whose protein core is similar to that of the b6f complex. Prior to X-ray crystal structure analysis, each monomeric unit of the complex was known to contain six bound prosthetic groups, three hemes (f, two hemes b, bp and bn), one [2Fe-2S] cluster, and one molecule each of chlorophyll-a and carotene. Crystal structure analysis of the b6f complex from a green alga and a thermophilic cyanobacterium revealed the presence of an additional heme cn in the complex, which is covalently bound on the ...
ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, autoinhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit ɛ adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme and engages both rotor and stator subunits in extensive contacts that are incompatible with functional rotation. As a result, the three catalytic subunits are stabilized in a set of conformations and rotational positions distinct from previous F(1) structures.. ...
Not only does cryo-EM offer exciting new possibilities, but the development of X-ray free-electron lasers (XFELs), and of serial crystallography at both XFEL and advanced synchrotron sources, now allow us to `tackle with relative ease complex biological structures or to take crystallography to unthinkably small time-frames and nanocrystals.Cited by: 1.
Description of x-ray crystallography research in the Chemical, Physical and Structural Biology Program in the Graduate School of Biomedical Sciences....
S100B is a homodimeric zinc-, copper-, and calcium-binding protein of the family of EF-hand S100 proteins. Zn(2+) binding to S100B increases its affinity towards Ca(2+) as well as towards target peptides and proteins. Cu(2+) and Zn(2+) bind presumably to the same site in S100B. We determined the structures of human Zn(2+)- and Ca(2+)-loaded S100B at pH 6.5, pH 9, and pH 10 by X-ray crystallography at 1.5, 1.4, and 1.65Å resolution, respectively. Two Zn(2+) ions are coordinated tetrahedrally at the dimer interface by His and Glu residues from both subunits. The crystal structures revealed that ligand swapping occurs for one of the four ligands in the Zn(2+)-binding sites. Whereas at pH 9, the Zn(2+) ions are coordinated by His15, His25, His 85, and His 90, at pH 6.5 and pH 10, His90 is replaced by Glu89. The results document that the Zn(2+)-binding sites are flexible to accommodate other metal ions such as Cu(2+). Moreover, we characterized the structural changes upon Zn(2+) binding, which ...
9780387333342 Our cheapest price for Principles of Protein X-Ray Crystallography is $77.18. Free shipping on all orders over $35.00.
Related Article: Li-Ming Yang, Shwu-Fen Chang, Wen-Kuang Lin, Bo-Hon Chou, Li-Hsuan Wang, Pan-Chun Liu, Shwu-Jiuan Lin,2012,Phytochemistry,75,90,doi:10.1016/j.phytochem.2011.12.006,An entry from the Cambridge Structural Database, the worlds repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures ...
The grant, from the Wellcome Trust, will enable the department to purchase a state-of-the-art CCD X-ray detector which it has had on loan from the manufacturers Bruker AXS for the past 3 years.. X-ray crystallography is the most widely-used method for solving the 3D structure of proteins. During the procedure, the X-rays are scattered by crystals of the protein and their pattern provides information about the shape of the molecule. The X-rays are detected using a highly efficient CCD detector.. The detector which has been on loan to the department is fast, efficient and easy to use. It has already enabled researchers to solve the structures of many important biomedical proteins including those involved in pathogen virulence, antibiotic biosynthesis, the cell division cycle and oxygen sensing.. In addition to high quality equipment, the X-ray facility relies on the support of the Facilities Manager, Dr Ed Lowe. Dr Lowe provides high level training and assistance to all users and maintains the ...
An entry from the Cambridge Structural Database, the worlds repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures ...
An entry from the Cambridge Structural Database, the worlds repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures ...
Vol 70: Purification, crystallization and preliminary X-ray crystallographic studies of Rv3705c from Mycobacterium tuberculosis.. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Crystal structures of lithium, sodium, potassium, calcium and magnesium salts of adenosine 2-monophosphate (2-AMP) have been obtained at atomic resolution by X-ray crystallographic methods. 2-AMP.Li belongs to the monoclinic space group P21 with a = 7.472(3)Å, b = 26.853(6) Å, c = 9.184(1)Å, b = 113.36(1)Å and Z= 4. 2-AMP.Na and 2-AMP.K crystallize in the trigonal space groups P31 and P3121 with a = 8.762(1)Å, c = 34.630(5)Å, Z= 6 and a = 8.931(4), Åc = 34.852(9)Å and Z= 6 respectively while 2-AMP.Ca and 2-AMP.Mg belong to space groups P6522 and P21 with cell parameters a = 9.487(2), c = 74.622(13), Z = 12 and a = 4.973(1), b = 10.023(2), c = 16.506(2), beta = 91.1(0) and Z = 2 respectively. All the structures were solved by direct methods and refined by full matrix least-squares to final R factors of 0.033, 0.028, 0.075, 0.069 and 0.030 for 2-AMP.Li, 2-AMP.Na, 2- AMP.K, 2-AMP.Ca and 2-AMP.Mg, respectively. The neutral adenine bases in all the structures are in syn ...
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The structure of the intact ATP synthase from the α-proteobacterium Paracoccus denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray crystallography at 4.0 Å resolution. The ζ-protein is bound via its N-terminal α-helix in a catalytic interface in the F1 domain. The bacterial F1 domain is attached to the membrane domain by peripheral and central stalks. The δ-subunit component of the peripheral stalk binds to the N-terminal regions of two α-subunits. The stalk extends via two parallel long α-helices, one in each of the related b and b′ subunits, down a noncatalytic interface of the F1 domain and interacts in an unspecified way with the a-subunit in the membrane domain. The a-subunit lies close to a ring of 12 c-subunits attached to the central stalk in the F1 domain, and, together, the central stalk and c-ring form the enzymes rotor. Rotation is driven by the transmembrane proton-motive force, by a mechanism where protons pass through the interface ...
The high resolution crystal structure of green abalone sperm lysin: Implications for species-specific binding of the egg receptor ...
Although the main research areas of interest at BioCARS are time-resolved macromolecular crystallography and structural studies of biohazards at the BSL-2 and BSL-3 level, BioCARS also offers the full range of standard macromolecular crystallography experiments such as: single wavelength, SAD and MAD, ultra-high resolution and large unit cell data collection. The 14-BM-C station, with a large Quantum-315 ADSC detector is particularly suitable and has been very successful in ultra-high resolution and large unit cell data collection.. Our flexible end-station setup and auxiliary equipment available to users permit non-standard experiments, for example those involving on-line micro-spectrophotometry, flow cell use and on-line illumination of samples by visible light from laser and other light sources. These tools are particularly important for kinetic crystallography (Bourgeois and Royant, 2005; Petsko and Ringe, 2000; Schlichting, 2000; Stoddard, 2001), where transient, intermediate states in the ...
article{2f5ed112-7711-4829-944a-2b87a0437947, abstract = {SUMMARY: The bacterial ω-transaminase from Chromobacterium violaceum (Cv-ωTA, EC 2.6.1.18) catalyzes industrially important transamination reactions by use of the coenzyme pyridoxal 5-phosphate (PLP). Here, we present four crystal structures of Cv-ωTA: two in the apo form, one in the holo form and one in an intermediate state, at resolutions between 1.35 and 2.4 Å. The enzyme is a homodimer with a molecular weight of approximately 100 kDa. Each monomer has an active site at the dimeric interface that involves amino acid residues from both subunits. The apo-Cv-ωTA structure reveals unique relaxed conformations of three critical loops involved in structuring the active site, that have not previously been seen in a transaminase. Analysis of the four crystal structures reveals major structural rearrangements involving elements of the large and small domains of both monomers that reorganize the active site in the presence of PLP. The ...
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt 4):419-21. doi: 10.1107/S1744309109008719. Epub 2009 Mar 26. Research Support, Non-U.S. Govt
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The crystal structure of the mineral tinticite has been solved by direct methods from integrated intensities of X-ray powder diffraction data and subsequently refined with the Rietveld technique. The sample used for the structure solution comes from the Gavá-Bruguers area (20 km SW of Barcelona), which contains a large variety of phosphates, some of which were exploited in gallery mines during the ancient neolithic. Tinticite crystallizes in the triclinic space group P1̄ with unit cell parameters a = 7.965(2) Å, b = 9.999(2) Å, c = 7.644(2) Å, α = 103.94(2)°, β = 115.91(2)°, ω = 67.86(2)° and cell content Fe3+5.34(PO4)3.62(VO4)0.38(OH)4·6.7 H2O; ρexp = 2.94 g/cm3; ρcale = 2.88 g/cm3. The Rietveld refinement of the data set converged to Rwp = 13.1 % and χ2 = 3.3. Due to the complexity of the disorder in this structure, the refined structure model could only account for part of it. The octahedrally coordinated Fe3+ ions form dreier single chains of general formula ∞1[Fe3O14] ...
A novel dioxygenase from AMMD (SadA) stereoselectively catalyzes the C3-hydroxylation of AMMD. put into the solution during purification and crystallization. The crystals were obtained by mixing 1.0 l protein solution with 1.0 l reservoir solution consisting of 0.1 M CHES (pH 9.5) and 30% (w/v) PEG 3,000 at 293 K. The purification and crystallization CCG-63802 of selenomethionine-substituted SadA (SadASeMet) were performed as reported previously [15]. The cosubstrate -KG was added to the protein treatment for a final concentration of 10 mM and was cocrystallized with SadA seed crystals under the same crystallization conditions. Data Collection and Processing The X-ray diffraction data of SadA.Zn(II) and SadA.Zn(II).-KG complex crystals were collected around the AR-NW12A and AR-NE3A beamlines at Photon Manufacturing plant (Tsukuba, Japan), respectively. For phasing by single-wavelength anomalous dispersion (SAD) of selenium atoms, we collected the X-ray diffraction CCG-63802 data of SadASeMet ...
Two different crystal forms of human thioredoxin peroxidase-B have been grown by vapour diffusion using polyethylene glycol 400 as a precipitant. Monoclinic P21 crystals were grown from freshly purified protein, whilst orthorhombic P212121 crystals were grown from purified protein that had been stored in ammonium sulfate, but otherwise under the same conditions. The diffraction from both crystal forms was observed to extend to beyond 2.0 A resolution using synchrotron radiation. Complete native data sets to 1.8 and 3. 7 A have been collected from the monoclinic and orthorhombic crystals, respectively.
Protein crystals are almost always grown in solution. The most common approach is to lower the solubility of its component molecules very gradually; if this is done too quickly, the molecules will precipitate from solution, forming a useless dust or amorphous gel on the bottom of the container. Crystal growth in solution is characterized by two steps: nucleation of a microscopic crystallite (possibly having only 100 molecules), followed by growth of that crystallite, ideally to a diffraction-quality crystal.[103] The solution conditions that favor the first step (nucleation) are not always the same conditions that favor the second step (subsequent growth). The crystallographers goal is to identify solution conditions that favor the development of a single, large crystal, since larger crystals offer improved resolution of the molecule. Consequently, the solution conditions should disfavor the first step (nucleation) but favor the second (growth), so that only one large crystal forms per droplet. ...
The laboratory of Chemistry of Biological Processes is equipped with state of the art devices for the crystallization of biological macromolecules. The laboratory houses a Mosquito® Crystal (TTPLabtech) that allows the automated screening of crystallization conditions using low sample volumes and zero cross-contaminations. The robot allows the setup of sitting and hanging drop vapor diffusion trials and can perform microbatch under oil if desired. Our laboratory also owns a 5-head Dragonfly® (TTPLabtech) as a companion for the Mosquito®, which allows the setup of crystallizations screens for crystal optimization. To check the crystallization experiments, two stereomicroscopes are available including a LEICA M205C equipped with a camera IC80 HD. ...
article{49551aab-f755-4e4a-89ae-3d0c95feca98, abstract = {A beamline for macromolecular crystallography is under construction at the Swedish synchrotron light source MAX-lab at Lund University in a collaborative effort between Denmark and Sweden. Of the 7 mrad horizontal wiggler fan emitted from the new superconducting multipole wiggler, the central 2 mrad will be used and split in three parts. The central 1 mrad will be used for a tunable station optimised for multi-wavelength anomalous diffraction experiments and on each side of the central fan there will be two fixed wavelength stations using different energies of the same part of the beam. These in total five stations can be used simultaneously and independently for collecting diffraction data.}, author = {Mammen, C B and Ursby, Thomas and Cerenius, Yngve and Thunnissen, Marjolein and Als-Nielsen, J and Larsen, S and Liljas, Anders}, issn = {0587-4246}, language = {eng}, number = {5}, pages = {595--602}, publisher = {Institute of Physics, ...
A novel metal-organic planar NiS4 - type complex, trans-Ni(II)-bis[O-(2-butoxyethyl)-(4-methoxyphenyl)dithiophosphonate], was synthesized by the reaction of ammonium salt of O-dithiophosphonic acid with Ni(CH3COO)(2). The crystal structure of Ni(II)-complex was determined by X-ray Diffraction (XRD) analysis. As a result of the X-ray crystal and molecule structure analyses of the studied trans-Ni(II)-complex, it was obtained that the central nickel atom is coordinated by four sulphur atoms in slightly distorted a square-planar geometry. The X-ray structure confirms a trans isomer of the Ni(II)complex. The Ni(II)-complex crystallizes in the monoclinic space group C12/c1 with unit cell parameters a 22.376(3) (angstrom), b 18.466(3) (angstrom) and c 8.6875(13) (angstrom). In addition, theoretical calculations with the basis set of B3LYP/6-311 + G(2d,p) are performed to determine the structural properties, FT-IR, NMR spectrum, electronic properties and NBO analysis of the compound. The experimental ...
TY - JOUR. T1 - Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP, a human 38-kDa apolipoprotein. AU - Diemer, Hélène. AU - Elias, Mikael. AU - Renault, Frédérique. AU - Rochu, Daniel. AU - Contreras-Martel, Carlos. AU - Schaeffer, Christine. AU - Van Dorsselaer, Alain. AU - Chabriere, Eric. PY - 2008/6. Y1 - 2008/6. N2 - The Human Phosphate Binding Protein (HPBP) is a serendipitously discovered apolipoprotein from human plasma that binds phosphate. Amino acid sequence relates HPBP to an intriguing protein family that seems ubiquitous in eukaryotes. These proteins, named DING according to the sequence of their four conserved N-terminal residues, are systematically absent from eukaryotic genome databases. As a consequence, HPBP amino acids sequence had to be first assigned from the electronic density map. Then, an original approach combining X-ray crystallography and mass spectrometry provides the complete and a ...
New Phasing HomeLab™ Solutions for Protein Crystallography Structure Determination Using Enhanced Anomalous Scattering Signals 642046618
Electron crystallography is a method to determine the arrangement of atoms in solids using an electron microscope. It can complement X-ray crystallography on proteins, such as membrane proteins, that cannot easily form the large 3-dimensional crystals required for that process. Structures are usually determined from either 2-dimensional crystals (sheets or helices), polyhedrons such as viral capsids, or dispersed individual proteins. Electrons can be used in these situations, whereas X-rays cannot, because electrons interact more strongly with atoms than X-rays do. Thus, X-rays will travel through a thin 2-dimensional crystal without diffracting significantly, whereas electrons can be used to form an image. Conversely, the strong interaction between electrons and proteins makes thick (e.g. 3-dimensional) crystals impervious to electrons, which only penetrate short distances. One of the main difficulties in X-ray crystallography is determining phases in the diffraction pattern. Because no X-ray ...
TY - JOUR. T1 - Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida. AU - Tu, Xiongying. AU - Latham, John A.. AU - Klema, Valerie J.. AU - Evans, Robert L.. AU - Li, Chao. AU - Klinman, Judith P.. AU - Wilmot, Carrie M.. PY - 2017/10/1. Y1 - 2017/10/1. N2 - PqqB is an enzyme involved in the biosynthesis of pyrroloquinoline quinone and a distal member of the metallo-β-lactamase (MBL) superfamily. PqqB lacks two residues in the conserved signature motif HxHxDH that makes up the key metal-chelating elements that can bind up to two metal ions at the active site of MBLs and other members of its superfamily. Here, we report crystal structures of PqqB bound to Mn2+, Mg2+, Cu2+, and Zn2+. These structures demonstrate that PqqB can still bind metal ions at the canonical MBL active site. The fact that PqqB can adapt its side chains to chelate a wide spectrum of metal ions with different coordination features on a uniform main chain ...
Single crystals of CaGeO3 garnet were synthesized at 3 GPa and 1000 °C using a cubic anvil type of high pressure apparatus and the crystal structure was refined from single crystal X-ray diffraction data. This garnet is tetragonal with lattice parameters of a = 12.535(2) Å, c = 12.370(2) Å, V = 1943.5(5) Å3 and belongs to space group I41/a. Two dodecahedral sites are occupied only by Ca with mean Ca-O bond lengths of 2.480(4) and 2.467(4) Å. The Ca and Ge cations are completely ordered at two octahedral sites with mean Ca-O = 2.301(3) Å and mean Ge-O = 1.910(3) Å. Three tetrahedral sites are occupied only by Ge, and their mean Ge-O bond lengths are 1.753(3), 1.787(4), and 1.764(4) Å. Furthermore, the present tetragonal garnet has an unusual feature in that the mean value [2.704(5) Å] of the shared edge lengths of GeO6 octahedron is larger than that [2.699(5) Å] of the unshared ones, as has also been observed for other tetragonal garnets with I41/a. ...
The addition-cyclocondensation reactions of three /?-hydroxyketones with four dialkyl phosphites gave 2-alkoxy-3-hydroxy-l,2-oxaphospholane-2-oxides (a-hydroxyphosto-nes) (7), in moderate yields. In the solid state and in solution, these compounds exist as dimers with hydrogen bonding between the hydroxyl group and the phosphoryl oxygen atom of an adjacent molecule. The crystal and molecular structure of 3-hydroxy-2-methoxy-3,5,5-trimethyl-l,2-oxaphospholane-2-oxide (7 a) has been determined by single-crystal X-ray crystallography: C7H15O4P, monoclinic space group P2-l/n, cell dimensions a = 8.087(1) Ä, b = 13.386(2) A, c = 9.306(1) A, V = 1007.4 Ä 3 , Z = 4, final R = 0.052. The five-membered ring is puckered, with the carbon bearing the OH and CH3 groups lying out of the plane of the remaining four atoms in the ring. The doubly bonded oxygen attached to the phosphorus atom and the hydroxyl oxygen are in a cis-relationship. The 0(l)-0(4) intermolecular bond distance of 2.75 Ä suggests ...
Serine-rich repeat proteins (SRRPs) belong to a growing family of bacterial adhesins required for biofilm formation and pathogenesis. Fap1 from Streptococcus parasanguinis is the first SRRP identified. A number of genes involved in Fap1 glycosylation have been characterized. Glycosyltransferases Gtf1, Gtf2 and Gtf3 catalyze the first and second steps of Fap1 glycosylation. A glycosyltransferase, GalT1, catalyzes the third step of Fap1 glycosylation. At the N-terminus of GalT1, there is a domain of unknown function 1792 (DUF1792) that is highly conserved in bacteria and may constitute a broad protein superfamily, however its function is unknown. Objective: Solve 3-D structure of DUF1792 to determine the function of the domain Method: The recombinant DUF1792 protein was purified via Ni2+ affinity chromatography and gel filtration. The hanging-drop vapor-diffusion method was used for the crystallization trials. The structure was determined by multiwavelength anomalous diffraction (MAD) utilizing Se ...
Recently some particularly keen crystallographers at Diamond filmed their visit to the beamline and posted it on youtube. Maybe not as amusing as the LHCs resident rapper, but this does give a brief glimpse into data collection practicalities for the modern structural biologist. ...
The common goal for structural genomic centers and consortiums is to decipher as quickly as possible the three-dimensional structures for a multitude of recombinant proteins derived from known genomic sequences. Since X-ray crystallography is the foremost method to acquire atomic resolution for macromolecules, the limiting step is obtaining protein crystals that can be useful of structure determination. High-throughput methods have been developed in recent years to clone, express, purify, crystallize and determine the three-dimensional structure of a protein gene product rapidly using automated devices, commercialized kits and consolidated protocols. However, the average number of protein structures obtained for most structural genomic groups has been very low compared to the total number of proteins purified. As more entire genomic sequences are obtained for different organisms from the three kingdoms of life, only the proteins that can be crystallized and whose structures can be obtained ...
The lectin from Bowringia mildbraedii seeds crystallizes in the presence of the disaccharide Man(alpha1-2)Man. The best crystals grow at 293 K within four weeks after a pre-incubation at 277 K to induce nucleation. A complete data set was collected to a resolution of 1.90 A using synchrotron radiation. The crystals belong to space group I222, with unit-cell parameters a = 66.06, b = 86.35, c = 91.76 A, and contain one lectin monomer in the asymmetric unit.. ...
Methods are described wherein crystallization conditions determined in a microfluidic device are translated into crystallization conditions in alternati...
The following examples show how to set up alternate conformations for structure factor calculations as well as for empirical energy calculations. The first step is to append the alternate conformations to the current molecular structure file. In this particular case, one wants to generate alternate conformations for the side chains of residues 1 and 7. alternate.inp Now one has to go to the graphics and move the alternate conformations into the correct positions. In subsequent protocols, one has to insert the following statement after reading the molecular structure file ...
Leucine-rich-alpha-2-glycoprotein1 (LRG1), a serum protein produced by hepatocytes, functions as a modulator of transforming growth factor beta1 (TGFβ1) signaling in angiogenesis and tumor progression. However, structural studies of LRG1 and detailed binding partners interactions have not been reported. To understand structural features and functions of LRG1, purification and crystallization of full length LRG1 were performed in the present study. The crystal of LRG1 diffracted X-rays at a resolution of 2.5 Å. The crystal belonged to space group P6322, having unit cell parameters of a = 143.02 Å, b = 143.02 Å, c = 113.73 Å, α = β = 90º, and γ = 120º with five LRG1 molecules present in the asymmetric unit ...
Crystallography Made Crystal Clear makes crystallography accessible to readers who have no prior knowledge of the field or its mathematical basis. This is the most comprehensive and concise reference for beginning Macromolecular crystallographers, written by a leading expert in the field. Rhodes uses visual and geometric models to help readers understand the mathematics that form the basis of x-ray crystallography. He has invested a great deal of time and effort on World Wide Web tools for users of models, including beginning-level tutorials in molecular modeling on personal computers. Rhodes personal CMCC Home Page also provides access to tools and links to resources discussed in the text. Most significantly, the final chapter introduces the reader to macromolecular modeling on personal computers-featuring SwissPdbViewer, a free, powerful modeling program now available for PC, Power Macintosh, and Unix computers. This updated and expanded new edition uses attractive four-color art, web tool access
The structure of orthorhombic crystals of monellin, a sweet protein extracted from African serendipity berries, has been solved by molecular replacement and refined to 2.3 A resolution. The final R factor was 0.150 for a model with excellent geometry. A monellin molecule consists of two peptides tha …
A series of thirteen isomeric 1,5-diphenylformazans have been structurally characterised both in the solid state and in solution by the combined techniques of x-ray crystallography, nuclear magnetic resonance, Raman, mass and absorption spectroscopies. 1,5-Diphenylformazan is known to exist in the anti, s-trans configuration in the solid state and this is shown to be the solution dominant species. In aprotic solvents an equilibrium involving the anti, s-trans and syn, s-cis configurations is evidenced. 3-Methyl-1,5-diphenylformazan has been characterised by an x-ray crystal analysis. C14H14N4 belongs to the monoclinic space group P2/c, a = 8.133(1), b = 19.085(4), c = 9.364(2) A, beta = 105.93 degrees,U = 1397.6(5) A3, Z = 4. The anti, s-trans configuration of the solid state is also preferred in solution where it is in equilibrium with the syn, s-cis configuration. 3-Ethyl-1,5-diphenylformazan exists in two isomers in the solid state, both of which have been characterised by an x-ray crystal ...
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Uad Plugins 64 Bit is a molecular viewer, render tool, 3D molecular editor developed in the spirit of RasMol and OpenRasMol and intended for visualization of 3D chemical structures including atomic resolution X-ray crystal structures of: proteins, nucleic acids (DNA, RNA, & tRNA), and carbohydrates, as well as small molecule structures of drug leads, inhibitors, metabolites, sugars, nucleoside phosphates, and other ligands including inorganic salts and solvent molecules. The familiar interface doesnt help the program run smoothly. The program is highly dependent on the system resources of the computers involved. Throw in varying Internet connection speeds and stability becomes a major problem. Mouse movements were usually more responsive than keyboard inputs, and read-only access runs smoother than edit-level permissions. Labels at the top of the remote screen make program status accessible. Uad Plugins 64 Bit itself handles any file transfers. Also, Uad Plugins 64 Bit has two help resources, a ...
TY - JOUR. T1 - Synthesis and Crystal and Molecular Structure of the Conformationally Restricted Methionine Analogue (±)-2-exo-Amino-6-endo-(methylthio)bicyclo[2.2.1]heptane-2-endo-carboxylic Acid and Neighboring Group Participation in its Anodic Oxidation. AU - Glass, Richard S.. AU - Hojjatie, Massoud. AU - Sabahi, Mahmood. AU - Steffen, L. Kraig. AU - Wilson, George S.. PY - 1990/1/1. Y1 - 1990/1/1. N2 - (±)-2-exo-Amino-6-endo-(methylthio)bicyclo[2.2.1]heptane-2-endo-carboxylic acid (lc) was synthesized by amination of the lithium enolate of methyl 6-endo-(methylthio)bicyclo[2.2.1]heptane-2-ercdo-carboxylate with 0-(mesitylenesulfonyl)hydroxylamine followed by hydrolysis. Its crystal and molecular structure was determined by single-crystal X-ray analysis. It crystallizes in the monoclinic space group P21/c with a = 9.681 (6) Å, b = 10.276 (5) Å, c = 9.773 (4) Å, β = 91.23 (4)°, and Z = 4. The structure was solved by direct methods. Full-matrix least-squares refinement led to a ...
The facility provides low volume crystallisation services and screen making. Our customers can also order custom built premixed crystallisation solutions. Full crystallisation service includes composition of the crystallisation setup and scheduled imaging of the experiment for up to four months. The crystallisation droplets are set up using our Mosquito LCP or Oryx nanodrop robots, which can use as little as 100 nl protein per experiment and are suitable for membrane proteins and for air-sensitive samples. Scientists can examine the maturation of the project over time and can pick up the crystallisation plate for an X-ray experiment. The facility is equipped with a dedicated imaging station for combined visible/UV epifluorescence imaging of very small protein crystals (2μm ...
6CTP: Ternary complex crystal structure of DNA polymerase Beta with a dideoxy terminated primer with CH2, beta, gamma dTTP analogue
6CTU: Ternary complex crystal structure of DNA polymerase Beta with a dideoxy terminated primer with CFCL, beta, gamma dCTP analogue
John Desmond Bernal, Irish physicist and crystallographer, 1952. by Rickard, Stephen. Museum quality art prints with a selection of frame and size options, canvases, postcards and mugs. SSPL Science and Society Picture Library
TY - JOUR. T1 - Short, strong hydrogen bonds on enzymes. T2 - NMR and mechanistic studies. AU - Mildvan, A. S.. AU - Massiah, M. A.. AU - Harris, T. K.. AU - Marks, G. T.. AU - Harrison, D. H.T.. AU - Viragh, C.. AU - Reddy, P. M.. AU - Kovach, I. M.. PY - 2002/9/26. Y1 - 2002/9/26. N2 - The lengths of short, strong hydrogen bonds (SSHBs) on enzymes have been determined with high precision (±0.05 Å) from the chemical shifts (δ), and independently from the D/H fractionation factors (φ) of the highly deshielded protons involved. These H-bond lengths agree well with each other and with those found by protein X-ray crystallography, within the larger errors of the latter method (±0.2 to ± 0.8 Å) [Proteins 35 (1999) 275]. A model dihydroxynaphthalene compound shows a SSHB of 2.54 ± 0.04 Å based on δ = 17.7 ppm and φ = 0.56 ± 0.04, in agreement with the high resolution X-ray distance of 2.55 ± 0.06 Å. On ketosteroid isomerase, a SSHB is found (2.50 ± 0.02 Å), based on δ = 18.2 ppm and ...
The structure of the synthetic deoxyoctamer d(GGIGCTCC) has been determined by single crystal X-ray diffraction techniques to a resolution of 1.7A. The sequence crystallises in space group P6(1), with unit cell dimensions a = b = 45.07, c = 45.49A. The refinement converged with a crystallographic residual R = 0.14 and the location of 81 solvent molecules. The octamer forms an A-DNA duplex with 6 Watson-Crick (G.C) base pairs and 2 inosine-thymine (I.T) pairs. Refinement of the structure shows it to be essentially isomorphous with that reported for d(GGGGCTCC) with the mispairs adopting a wobble conformation. Conformational parameters and base stacking interactions are compared to those for the native duplex d(GGGGCCCC) and other similar sequences. A rationale for the apparent increased crystal packing efficiency and lattice stability of the I.T octamer is given. Refined crystal structure of an octanucleotide duplex with I.T. mismatched base pairs.,Cruse WB, Aymani J, Kennard O, Brown T, Jack ...
Crystallization is the major bottleneck to 3D structure determination using X-ray crystallography. In this workshop we will discuss many tenets of successful crystallization for both conventional and serial crystallography. Many topics will be covered including fundamentals of crystal growth, strategies to sample crystallization space, identifying crystal hits, electron microscopy applications of crystal analysis, practical considerations for data analysis, difficult crystallization problems, virus crystallography, and an overview of serial crystallography.
Ranasmurfin, a previously uncharacterized similar to 13 kDa blue protein found in the nests of the frog Polypedates leucomystax, has been purified and crystallized. The crystals are an intense blue colour and diffract to 1.51 angstrom with P2(1) symmetry and unit-cell parameters a = 40.9, b = 59.9, c = 45.0 angstrom, beta = 93.3 degrees. Self-rotation function analysis indicates the presence of a dimer in the asymmetric unit. Biochemical data suggest that the blue colour of the protein is related to dimer formation. Sequence data for the protein are incomplete, but thus far have identified no model for molecular replacement. A fluorescence scan shows a peak at 9.676 keV, indicating that the protein binds zinc and suggesting a route for structure solution ...
Tup1cΔ crystals were grown by hanging‐drop vapor diffusion by mixing an equal volume of protein and reservoir solution containing 50‐100 mM bis‐Tris propane pH 9, 0‐50 mM NaCl, 23‐26% (w/v) polyethylene glycol 6000 and 2 mM dithiothreitol or 1 mM BMS, and allowing the drop to equilibrate with the reservoir at 20°C. Crystals grew to an average size of 0.1 × 0.1 × 1 mm in ∼1 week. Native crystals were transferred to a drop containing well solution immediately prior to data collection. Heavy‐atom derivatives were prepared by soaking crystals in a solution containing 50 mM bis‐Tris propane pH 9 and 24% (w/v) PEG 6000 with the heavy‐atom reagent (0.5 mM EMTS for 12 h, 1 mM KAu(CN)2 for 22 h or 0.5 mM PIP for 12 h). Data were collected at room temperature on a RAXIS IIc detector equipped with a rotating‐anode Rigaku RU‐200 generator with CuKα radiation. Attempts to cryocool the crystals at −180°C were unsuccessful. All data were integrated and reduced using the ...
Mpr1 is an enzyme that catalyzes the N‐acetylation of the toxic l‐azetidine‐2‐carboxylic acid (AZC). Recently, Mpr1 has been shown to reduce levels of intracellular reactive oxygen species (ROS) under oxidative stress. The natural substrate involved in the ROS elimination in vivo is still unknown. Mpr1 has been purified and crystallized in space groups P1 and P3112. X‐ray data were collected to 1.9 Å resolution from a trigonal crystal soaked with AZC ...
TY - JOUR. T1 - Synthesis and crystal and molecular structure of [(nC4H9)4N]2[MoO2(C5O5)2]; confirmation of exclusively η2-coordination by a croconate ligand. AU - Chen, Qin. AU - Liu, Shuncheng. AU - Zubieta, Jon. N1 - Funding Information: The research was supported by a grant from the National Science Foundation (CHE8815299).. PY - 1990/9/17. Y1 - 1990/9/17. N2 - The reaction of [(nC4H9)4N]2[Mo2O7] with BaC5O5 in acetonitrile yields red crystals of [(n C4H9)4N]2[MoO2(C5O5)2]. The compound crystallizes in the monoclinic space group C2/c with a=36.502(11), b=14.681(3), c=18.109(5) Å, β=93.84(1)°, V=9682.5(15) Å3, Dcalc=1.22 g cm-3 for Z=8. Structure solution and refinement based on 3593 reflections with Fo≥6σ(Fo) Mo Kα, λ= 0.71073 Å) converged at 0.0693. The structure of the anion consists of a mononuclear Mo(VI) center in ar distorted octahedral environment of the cis-oxo groups and the oxygen donors of two bidentate croconate ligands. The 1,2-chelating geometry of the croconate is ...
D. A. Erlanson Introduction to Fragment-Based Drug Discovery T. G. Davies Ian J. Tickle Fragment Screening Using X-Ray Crystallography S. Roughley L. Wright P. Brough A. Massey R. E. Hubbard Hsp90 Inh