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	<title>2021Cheng Native - Revision history</title>
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	<updated>2026-05-24T19:35:26Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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	<entry>
		<id>https://3demmethods.i2pc.es/index.php?title=2021Cheng_Native&amp;diff=4507&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  Cheng, Jing / Li, Bufan / Si, Long / Zhang, Xinzheng. Determining structures in a native environment using single-particle cryoelectron microscopy images. 2021...&quot;</title>
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		<updated>2024-01-08T07:11:59Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Cheng, Jing / Li, Bufan / Si, Long / Zhang, Xinzheng. Determining structures in a native environment using single-particle cryoelectron microscopy images. 2021...&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;
Cheng, Jing / Li, Bufan / Si, Long / Zhang, Xinzheng. Determining structures in a native environment using single-particle cryoelectron microscopy images. 2021. The Innovation, Vol. 2, No. 4, p. 100166&lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Cryo-electron tomography is a powerful tool for structure determination&lt;br /&gt;
in the native environment. However, this method requires the acquisition&lt;br /&gt;
of tilt series, which is time-consuming and severely slows structure&lt;br /&gt;
determination. By treating the densities of non-target protein as non-&lt;br /&gt;
Gaussian noise, we developed a new target function that greatly improves&lt;br /&gt;
the efficiency of recognizing the target protein in a single cryoelectron&lt;br /&gt;
microscopy image. Moreover, we developed a sorting function&lt;br /&gt;
that effectively eliminates the model dependence and improved the resolution&lt;br /&gt;
during the subsequent structure refinement procedure. By&lt;br /&gt;
eliminating model bias, our method allows using homolog proteins as&lt;br /&gt;
models to recognize the target proteins in a complex context. Together,&lt;br /&gt;
we developed an in situ single-particle analysis method. Our method was&lt;br /&gt;
successfully applied to solve structures of glycoproteins on the surface&lt;br /&gt;
of a non-icosahedral virus and Rubisco inside the carboxysome. Both&lt;br /&gt;
data were collected within 24 h, thus allowing fast and simple structural&lt;br /&gt;
determination.&lt;br /&gt;
&lt;br /&gt;
== Keywords ==&lt;br /&gt;
&lt;br /&gt;
== Links ==&lt;br /&gt;
&lt;br /&gt;
https://www.sciencedirect.com/science/article/pii/S2666675821000916&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>
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