3u7t: Difference between revisions
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The | ==Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin== | ||
<StructureSection load='3u7t' size='340' side='right'caption='[[3u7t]], [[Resolution|resolution]] 0.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3u7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U7T FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.85Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3u7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u7t OCA], [https://pdbe.org/3u7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u7t RCSB], [https://www.ebi.ac.uk/pdbsum/3u7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u7t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 A resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D-exchanged crambin crystal collected at the Protein Crystallography Station (PCS) showed diffraction beyond 1.1 A resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures. | |||
Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin.,Chen JC, Fisher Z, Kovalevsky AY, Mustyakimov M, Hanson BL, Zhurov VV, Langan P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt, 2):119-23. Epub 2012 Jan 21. PMID:22297981<ref>PMID:22297981</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3u7t" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Crambe hispanica subsp. abyssinica]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen JC-H]] | |||
Latest revision as of 02:29, 21 November 2024
Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin
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