3u7t

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'''Unreleased structure'''
 
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The entry 3u7t is ON HOLD
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==Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin==
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<StructureSection load='3u7t' size='340' side='right'caption='[[3u7t]], [[Resolution|resolution]] 0.85&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.85&#8491;</td></tr>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Chen, J.C.-H.
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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>
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Description: Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3u7t" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Crambe hispanica subsp. abyssinica]]
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[[Category: Large Structures]]
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[[Category: Chen JC-H]]

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Room temperature ultra-high resolution time-of-flight neutron and X-ray diffraction studies of H/D exchanged crambin

PDB ID 3u7t

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