8ew2

</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=8ew2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ew2 OCA], [https://pdbe.org/8ew2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ew2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ew2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ew2 ProSAT]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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