https://3demmethods.i2pc.es/index.php?action=history&feed=atom&title=2021Zhang_Pegylation 2026-05-24T21:14:37Z Revision history for this page on the wiki MediaWiki 1.44.2 https://3demmethods.i2pc.es/index.php?title=2021Zhang_Pegylation&diff=4089&oldid=prev 2021-10-22T06:55:13Z

<p>Created page with &quot;== Citation == 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....&quot;</p> <p><b>New page</b></p><div>== Citation ==<br /> <br /> Zhang, Z.; Shigematsu, H.; Shimizu, T. &amp;amp; Ohto, U. Improving particle quality in cryo-EM analysis using a PEGylation method. Structure, 2021, 29, 1192-1199.e4 <br /> <br /> == Abstract ==<br /> <br /> 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 /> <br /> == Keywords ==<br /> <br /> == Links ==<br /> <br /> https://www.sciencedirect.com/science/article/pii/S0969212621001623<br /> <br /> == Related software ==<br /> <br /> == Related methods ==<br /> <br /> == Comments ==</div>

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