<?xml version="1.0"?>
<feed xmlns="http://www.w3.org/2005/Atom" xml:lang="en">
	<id>https://3demmethods.i2pc.es/index.php?action=history&amp;feed=atom&amp;title=2018Bartesaghi_Refinement</id>
	<title>2018Bartesaghi Refinement - Revision history</title>
	<link rel="self" type="application/atom+xml" href="https://3demmethods.i2pc.es/index.php?action=history&amp;feed=atom&amp;title=2018Bartesaghi_Refinement"/>
	<link rel="alternate" type="text/html" href="https://3demmethods.i2pc.es/index.php?title=2018Bartesaghi_Refinement&amp;action=history"/>
	<updated>2026-05-24T20:20:43Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
	<generator>MediaWiki 1.44.2</generator>
	<entry>
		<id>https://3demmethods.i2pc.es/index.php?title=2018Bartesaghi_Refinement&amp;diff=3313&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Bartesaghi, A.; Aguerrebere, C.; Falconieri, V.; Banerjee, S.; Earl, L. A.; Zhu, X.; Grigorieff, N.; Milne, J. L. S.; Sapiro, G.; Wu, X. &amp; Subramaniam, S. Atom...&quot;</title>
		<link rel="alternate" type="text/html" href="https://3demmethods.i2pc.es/index.php?title=2018Bartesaghi_Refinement&amp;diff=3313&amp;oldid=prev"/>
		<updated>2018-05-27T09:03:53Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Bartesaghi, A.; Aguerrebere, C.; Falconieri, V.; Banerjee, S.; Earl, L. A.; Zhu, X.; Grigorieff, N.; Milne, J. L. S.; Sapiro, G.; Wu, X. &amp;amp; Subramaniam, S. Atom...&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;
Bartesaghi, A.; Aguerrebere, C.; Falconieri, V.; Banerjee, S.; Earl, L. A.; Zhu, X.; Grigorieff, N.; Milne, J. L. S.; Sapiro, G.; Wu, X. &amp;amp; Subramaniam, S. Atomic Resolution Cryo-EM Structure of β-Galactosidase. Structure, 2018 &lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
The advent of direct electron detectors has enabled the routine use of single-particle cryo-electron microscopy (EM) approaches to determine structures of a variety of protein complexes at near-atomic resolution. Here, we report the development of methods to account for local variations in defocus and beam-induced drift, and the implementation of a data-driven dose compensation scheme that significantly improves the extraction of high-resolution information recorded during exposure of the specimen to the electron beam. These advances enable determination of a cryo-EM density map for β-galactosidase bound to the inhibitor phenylethyl β-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at ∼ 1.5 Å resolution. Using this density map in conjunction with constrained molecular dynamics simulations provides a measure of the local flexibility of the non-covalently bound inhibitor and offers further opportunities for structure-guided inhibitor design.&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/abstract/S0969-2126(18)30129-1&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>
	</entry>
</feed>