8hi2
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of EV71 VLP frozen at -183 degree embedded in crystalline ice== | |
| + | <StructureSection load='8hi2' size='340' side='right'caption='[[8hi2]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8hi2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HI2 FirstGlance]. <br> | ||
| + | </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=8hi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hi2 OCA], [https://pdbe.org/8hi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hi2 RCSB], [https://www.ebi.ac.uk/pdbsum/8hi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hi2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A2D2CKV5_HE71 A0A2D2CKV5_HE71] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions. | ||
| - | + | Addressing compressive deformation of proteins embedded in crystalline ice.,Shi H, Wu C, Zhang X Structure. 2022 Dec 14:S0969-2126(22)00487-7. doi: 10.1016/j.str.2022.12.001. PMID:36586403<ref>PMID:36586403</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8hi2" style="background-color:#fffaf0;"></div> |
| - | [[Category: Shi | + | == References == |
| - | [[Category: Zhang | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Enterovirus A71]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Shi H]] | ||
| + | [[Category: Wu C]] | ||
| + | [[Category: Zhang X]] | ||
Revision as of 11:26, 1 February 2023
Structure of EV71 VLP frozen at -183 degree embedded in crystalline ice
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