http://3demmethods.i2pc.es/index.php?title=2021Zhang_Pegylation&feed=atom&action=history2021Zhang Pegylation - Revision history2024-03-29T15:16:09ZRevision history for this page on the wikiMediaWiki 1.29.1http://3demmethods.i2pc.es/index.php?title=2021Zhang_Pegylation&diff=4089&oldid=prevWikiSysop: Created page with "== Citation == Zhang, Z.; Shigematsu, H.; Shimizu, T. & Ohto, U. Improving particle quality in cryo-EM analysis using a PEGylation method. Structure, 2021, 29, 1192-1199...."2021-10-22T06:55:13Z<p>Created page with "== Citation == Zhang, Z.; Shigematsu, H.; Shimizu, T. & Ohto, U. Improving particle quality in cryo-EM analysis using a PEGylation method. Structure, 2021, 29, 1192-1199...."</p>
<p><b>New page</b></p><div>== Citation ==<br />
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Zhang, Z.; Shigematsu, H.; Shimizu, T. &amp; Ohto, U. Improving particle quality in cryo-EM analysis using a PEGylation method. Structure, 2021, 29, 1192-1199.e4 <br />
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== Abstract ==<br />
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Cryo-electron microscopy (cryo-EM) is widely used for structural biology studies and has been developed extensively in recent years. However, its sample vitrification process is a major limitation because it causes severe particle aggregation and/or denaturation. This effect is thought to occur because particles tend to stick to the “deadly” air-water interface during vitrification. Here, we report a method for PEGylation of proteins that can efficiently protect particles against such problems during vitrification. This method alleviates the laborious process of fine-tuning the vitrification conditions, allowing for analysis of samples that would otherwise be discarded. <br />
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== Links ==<br />
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https://www.sciencedirect.com/science/article/pii/S0969212621001623<br />
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== Comments ==</div>WikiSysop