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	<title>2026Mulvaney CASP16 - Revision history</title>
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	<updated>2026-04-29T03:11:41Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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	<entry>
		<id>https://3demmethods.i2pc.es/index.php?title=2026Mulvaney_CASP16&amp;diff=5136&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Mulvaney, T., Kryshtafovych, A. and Topf, M. 2026. Cryo-EM Analysis in CASP16. Proteins: Structure, Function, and Bioinformatics. (2026).  == Abstract ==  Since CASP13, experimentalists have been encouraged to provide their cryo-EM data along with the derived atomic models to the CASP organizers to aid assessment. In CASP16, 38 cryo-EM datasets were provided for assessment, which represented most cryo-EM targets. The corresponding targets typically compri...&quot;</title>
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		<updated>2026-01-07T08:14:42Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Mulvaney, T., Kryshtafovych, A. and Topf, M. 2026. Cryo-EM Analysis in CASP16. Proteins: Structure, Function, and Bioinformatics. (2026).  == Abstract ==  Since CASP13, experimentalists have been encouraged to provide their cryo-EM data along with the derived atomic models to the CASP organizers to aid assessment. In CASP16, 38 cryo-EM datasets were provided for assessment, which represented most cryo-EM targets. The corresponding targets typically compri...&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;
Mulvaney, T., Kryshtafovych, A. and Topf, M. 2026. Cryo-EM Analysis in CASP16. Proteins: Structure, Function, and Bioinformatics. (2026).&lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Since CASP13, experimentalists have been encouraged to provide their cryo-EM&lt;br /&gt;
data along with the derived atomic models to&lt;br /&gt;
the CASP organizers to aid assessment. In CASP16, 38 cryo-EM&lt;br /&gt;
datasets were provided for assessment, which represented most&lt;br /&gt;
cryo-EM&lt;br /&gt;
targets. The corresponding targets typically comprised a single derived atomic structure; however, that model may be&lt;br /&gt;
only one of several valid conformations. Flexibility often manifests as low-resolution&lt;br /&gt;
regions in a cryo-EM&lt;br /&gt;
reconstruction, particularly&lt;br /&gt;
in RNA but often also in protein complexes. We show that local resolution in the reconstruction correlates well with the&lt;br /&gt;
root-mean-&lt;br /&gt;
square&lt;br /&gt;
fluctuations (RMSF) of residues of accurate CASP predictions. The correlation between the local resolution&lt;br /&gt;
and pLDDT was less clear, especially when mobile domains were present. When the resolution allowed, assessment of features&lt;br /&gt;
such as sidechains, using our variant of SMOC with local fragment alignment, indicated that even high-quality&lt;br /&gt;
predictions have&lt;br /&gt;
room for improvement; on the other hand, some predictions fitted the density better in specific regions, indicating modeling&lt;br /&gt;
discrepancies in the target. In one extreme case, a submitted target had regions of low-resolution&lt;br /&gt;
that limited unambiguous&lt;br /&gt;
model building. In such cases, part of the target structure is essentially a prediction itself, with implications for the assessment.&lt;br /&gt;
Experimental data remain essential for model-free&lt;br /&gt;
assessment of predictions and offer unique analyses such as comparisons to&lt;br /&gt;
local resolution and thus flexibility.&lt;br /&gt;
&lt;br /&gt;
== Keywords ==&lt;br /&gt;
&lt;br /&gt;
== Links ==&lt;br /&gt;
&lt;br /&gt;
https://onlinelibrary.wiley.com/doi/full/10.1002/prot.70099&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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