5vnq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Neutron crystallographic strucutre of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature== | |
| + | <StructureSection load='5vnq' size='340' side='right' caption='[[5vnq]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vnq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VNQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vnr|5vnr]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vnq OCA], [http://pdbe.org/5vnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vnq RCSB], [http://www.ebi.ac.uk/pdbsum/5vnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vnq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteriophage T4 lysozyme (T4L) has been used as a paradigm for seminal biophysical studies on protein structure, dynamics, and stability. Approximately 700 mutants of this protein and their respective complexes have been characterized by X-ray crystallography; however, despite the high resolution diffraction limits attained in several studies, no hydrogen atoms were reported being visualized in the electron density maps. To address this, a 2.2 A-resolution neutron data set was collected at 80 K from a crystal of perdeuterated T4L pseudo-wild type. We describe a near complete atomic structure of T4L, which includes the positions of 1737 hydrogen atoms determined by neutron crystallography. The cryogenic neutron model reveals explicit detail of the hydrogen bonding interactions in the protein, in addition to the protonation states of several important residues. | ||
| - | + | Neutron crystallographic studies of T4 lysozyme at cryogenic temperature.,Li L, Shukla S, Meilleur F, Standaert RF, Pierce J, Myles DAA, Cuneo MJ Protein Sci. 2017 Oct;26(10):2098-2104. doi: 10.1002/pro.3231. Epub 2017 Sep 6. PMID:28707382<ref>PMID:28707382</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5vnq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lysozyme]] | ||
| + | [[Category: Cuneo, M J]] | ||
| + | [[Category: Li, L]] | ||
[[Category: Meilleur, F]] | [[Category: Meilleur, F]] | ||
| - | [[Category: | + | [[Category: Myles, D A.A]] |
[[Category: Pierce, J]] | [[Category: Pierce, J]] | ||
| - | [[Category: | + | [[Category: Shukla, S]] |
| - | [[Category: Standaert, R | + | [[Category: Standaert, R F]] |
| - | [[Category: | + | [[Category: Hydrogen bond]] |
| + | [[Category: Hydrogen bonding network]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Neutron crystallography]] | ||
| + | [[Category: T4 lysozyme]] | ||
| + | [[Category: Water]] | ||
Revision as of 09:08, 4 October 2017
Neutron crystallographic strucutre of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature
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