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	<title>2026Chen CryoEvoBuild - Revision history</title>
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	<updated>2026-04-15T04:56:10Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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	<entry>
		<id>https://3demmethods.i2pc.es/index.php?title=2026Chen_CryoEvoBuild&amp;diff=5159&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Chen, J., Li, T., He, J. and Huang, S.-Y. 2026. Protein model building for intermediate-resolution cryo-EM maps by integrating evolutionary and experimental information. Structure. 34, (2026), 375–384.  == Abstract ==  Accurate model building in intermediate-resolution cryo-EM maps normally requires flexible fitting of reliable initial structures. However, while deep learning-based methods such as AlphaFold2 can predict highly accurate structures, the p...&quot;</title>
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		<updated>2026-02-17T04:51:20Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Chen, J., Li, T., He, J. and Huang, S.-Y. 2026. Protein model building for intermediate-resolution cryo-EM maps by integrating evolutionary and experimental information. Structure. 34, (2026), 375–384.  == Abstract ==  Accurate model building in intermediate-resolution cryo-EM maps normally requires flexible fitting of reliable initial structures. However, while deep learning-based methods such as AlphaFold2 can predict highly accurate structures, the p...&amp;quot;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;== Citation ==&lt;br /&gt;
&lt;br /&gt;
Chen, J., Li, T., He, J. and Huang, S.-Y. 2026. Protein model building for intermediate-resolution cryo-EM maps by integrating evolutionary and experimental information. Structure. 34, (2026), 375–384.&lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Accurate model building in intermediate-resolution cryo-EM maps normally requires flexible fitting of reliable&lt;br /&gt;
initial structures. However, while deep learning-based methods such as AlphaFold2 can predict highly accurate&lt;br /&gt;
structures, the predicted structures often differ from experimental EM maps on both global and local&lt;br /&gt;
scales, which poses a great challenge to accurate model building in intermediate-resolution EM maps with&lt;br /&gt;
such initial structures. Addressing the challenge, we propose CryoEvoBuild, an automated method for&lt;br /&gt;
improved protein model building from intermediate-resolution EM maps through the effective integration&lt;br /&gt;
of evolutionary and experimental information. CryoEvoBuild implements a novel domain-wise fitting, refinement,&lt;br /&gt;
assembly, and rebuilding pipeline with a recycling framework guided by AlphaFold2. Extensive benchmarking&lt;br /&gt;
on a diverse test set of 117 maps at 4.0–10.0 A˚ resolutions demonstrates that CryoEvoBuild significantly&lt;br /&gt;
improves the accuracy of AF2-predicted structures and outperforms state-of-the-art approaches,&lt;br /&gt;
including EMBuild and phenix.dock_and_rebuild.&lt;br /&gt;
&lt;br /&gt;
== Keywords ==&lt;br /&gt;
&lt;br /&gt;
== Links ==&lt;br /&gt;
&lt;br /&gt;
https://www.cell.com/structure/fulltext/S0969-2126(25)00438-1&lt;br /&gt;
&lt;br /&gt;
== Related software ==&lt;br /&gt;
&lt;br /&gt;
== Related methods ==&lt;br /&gt;
&lt;br /&gt;
== Comments ==&lt;/div&gt;</summary>
		<author><name>WikiSysop</name></author>
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