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	<title>2024Lytje SAXS - Revision history</title>
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	<updated>2026-05-24T21:14:21Z</updated>
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		<id>https://3demmethods.i2pc.es/index.php?title=2024Lytje_SAXS&amp;diff=4683&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Lytje, Kristian / Pedersen, Jan Skov. Validation of electron-microscopy maps using solution small-angle X-ray scattering. 2024. Acta Crystallographica Section D: Structural Biology, Vol. 80, No. 7, p. 493-505  == Abstract ==  The determination of the atomic resolution structure of biomacromolecules is essential for understanding details of their function. Traditionally, such a structure determination has been performed with crystallographic or nuclear res...&quot;</title>
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		<updated>2024-08-13T06:50:54Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Lytje, Kristian / Pedersen, Jan Skov. Validation of electron-microscopy maps using solution small-angle X-ray scattering. 2024. Acta Crystallographica Section D: Structural Biology, Vol. 80, No. 7, p. 493-505  == Abstract ==  The determination of the atomic resolution structure of biomacromolecules is essential for understanding details of their function. Traditionally, such a structure determination has been performed with crystallographic or nuclear res...&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;
Lytje, Kristian / Pedersen, Jan Skov. Validation of electron-microscopy maps using solution small-angle X-ray scattering. 2024. Acta Crystallographica Section D: Structural Biology, Vol. 80, No. 7, p. 493-505&lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
The determination of the atomic resolution structure of biomacromolecules&lt;br /&gt;
is essential for understanding details of their function. Traditionally, such a&lt;br /&gt;
structure determination has been performed with crystallographic or nuclear&lt;br /&gt;
resonance methods, but during the last decade, cryogenic transmission electron&lt;br /&gt;
microscopy (cryo-TEM) has become an equally important tool. As the blotting&lt;br /&gt;
and flash-freezing of the samples can induce conformational changes, external&lt;br /&gt;
validation tools are required to ensure that the vitrified samples are representative&lt;br /&gt;
of the solution. Although many validation tools have already been&lt;br /&gt;
developed, most of them rely on fully resolved atomic models, which prevents&lt;br /&gt;
early screening of the cryo-TEM maps. Here, a novel and automated method&lt;br /&gt;
for performing such a validation utilizing small-angle X-ray scattering&lt;br /&gt;
measurements, publicly available through the new software package AUSAXS,&lt;br /&gt;
is introduced and implemented. The method has been tested on both simulated&lt;br /&gt;
and experimental data, where it was shown to work remarkably well as a validation&lt;br /&gt;
tool. The method provides a dummy atomic model derived from the EM&lt;br /&gt;
map which best represents the solution structure.&lt;br /&gt;
&lt;br /&gt;
== Keywords ==&lt;br /&gt;
&lt;br /&gt;
== Links ==&lt;br /&gt;
&lt;br /&gt;
https://journals.iucr.org/d/issues/2024/07/00/wan5003/&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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