View source for 9ewk


==Solvent organization in ultrahigh-resolution protein crystal structure at room temperature==
<StructureSection load='9ewk' size='340' side='right'caption='[[9ewk]], [[Resolution|resolution]] 0.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ewk]] 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=9EWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9EWK 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]] 0.7&#8491;</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=9ewk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ewk OCA], [https://pdbe.org/9ewk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ewk RCSB], [https://www.ebi.ac.uk/pdbsum/9ewk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ewk 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.
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== Publication Abstract from PubMed ==
Ultrahigh-resolution structures provide unprecedented details about protein dynamics, hydrogen bonding and solvent networks. The reported 0.70 A, room-temperature crystal structure of crambin is the highest-resolution ambient-temperature structure of a protein achieved to date. Sufficient data were collected to enable unrestrained refinement of the protein and associated solvent networks using SHELXL. Dynamic solvent networks resulting from alternative side-chain conformations and shifts in water positions are revealed, demonstrating that polypeptide flexibility and formation of clathrate-type structures at hydrophobic surfaces are the key features endowing crambin crystals with extraordinary diffraction power.

Solvent organization in the ultrahigh-resolution crystal structure of crambin at room temperature.,Chen JCH, Gilski M, Chang C, Borek D, Rosenbaum G, Lavens A, Otwinowski Z, Kubicki M, Dauter Z, Jaskolski M, Joachimiak A IUCrJ. 2024 Sep 1;11(Pt 5):649-663. doi: 10.1107/S2052252524007784. PMID:39190507<ref>PMID:39190507</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9ewk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Crambe hispanica subsp. abyssinica]]
[[Category: Large Structures]]
[[Category: Borek D]]
[[Category: Chang C]]
[[Category: Chen JC-H]]
[[Category: Dauter Z]]
[[Category: Gilski M]]
[[Category: Jaskolski M]]
[[Category: Joachimiak A]]
[[Category: Kubicki M]]
[[Category: Lavens A]]
[[Category: Otwinowski Z]]
[[Category: Rosenbaum G]]