https://3demmethods.i2pc.es/index.php?action=history&feed=atom&title=2023Shi_Compression2023Shi Compression - Revision history2026-06-13T12:11:45ZRevision history for this page on the wikiMediaWiki 1.44.2https://3demmethods.i2pc.es/index.php?title=2023Shi_Compression&diff=4964&oldid=prevWikiSysop: Created page with "== Citation == H. Shi, C. Wu, and X. Zhang, “Addressing compressive deformation of proteins embedded in crystalline ice,” Structure, vol. 31, no. 2, pp. 213–220, 2023. == Abstract == 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, s..."2025-04-14T10:29:26Z<p>Created page with "== Citation == H. Shi, C. Wu, and X. Zhang, “Addressing compressive deformation of proteins embedded in crystalline ice,” Structure, vol. 31, no. 2, pp. 213–220, 2023. == Abstract == 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, s..."</p>
<p><b>New page</b></p><div>== Citation ==<br />
<br />
H. Shi, C. Wu, and X. Zhang, “Addressing compressive deformation of proteins embedded in crystalline ice,” Structure, vol. 31, no. 2, pp. 213–220, 2023.<br />
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== Abstract ==<br />
<br />
For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein<br />
samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and<br />
how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used<br />
to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed<br />
at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples<br />
having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline<br />
ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a<br />
marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations<br />
and was essential for high-resolution reconstructions.<br />
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== Keywords ==<br />
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== Links ==<br />
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https://www.cell.com/structure/fulltext/S0969-2126(22)00487-7<br />
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== Related software ==<br />
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== Related methods ==<br />
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== Comments ==</div>WikiSysop