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	<id>https://3demmethods.i2pc.es/index.php?action=history&amp;feed=atom&amp;title=2024Karimi_Vesicle</id>
	<title>2024Karimi Vesicle - Revision history</title>
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	<updated>2026-05-01T09:51:57Z</updated>
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		<id>https://3demmethods.i2pc.es/index.php?title=2024Karimi_Vesicle&amp;diff=4865&amp;oldid=prev</id>
		<title>WikiSysop: Created page with &quot;== Citation ==  R. Karimi, C. E. Coupland, and J. L. Rubinstein, “Vesicle Picker: A tool for efficient identification of membrane protein complexes in vesicles,” J. Structural Biology, vol. 216, no. 4, p. 108148, 2024.  == Abstract ==  Electron cryomicroscopy (cryo-EM) has recently allowed determination of near-atomic resolution structures of membrane proteins and protein complexes embedded in lipid vesicles. However, particle selection from electron micrographs of t...&quot;</title>
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		<updated>2024-12-12T08:40:23Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  R. Karimi, C. E. Coupland, and J. L. Rubinstein, “Vesicle Picker: A tool for efficient identification of membrane protein complexes in vesicles,” J. Structural Biology, vol. 216, no. 4, p. 108148, 2024.  == Abstract ==  Electron cryomicroscopy (cryo-EM) has recently allowed determination of near-atomic resolution structures of membrane proteins and protein complexes embedded in lipid vesicles. However, particle selection from electron micrographs of t...&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;
R. Karimi, C. E. Coupland, and J. L. Rubinstein, “Vesicle Picker: A tool for efficient identification of membrane protein complexes in vesicles,” J. Structural Biology, vol. 216, no. 4, p. 108148, 2024.&lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Electron cryomicroscopy (cryo-EM) has recently allowed determination of near-atomic resolution structures of&lt;br /&gt;
membrane proteins and protein complexes embedded in lipid vesicles. However, particle selection from electron&lt;br /&gt;
micrographs of these vesicles can be challenging due to the strong signal contributed from the lipid bilayer. This&lt;br /&gt;
challenge often requires iterative and laborious particle selection workflows to generate a dataset of high-quality&lt;br /&gt;
particle images for subsequent analysis. Here we present Vesicle Picker, an open-source program built on the&lt;br /&gt;
Segment Anything model. Vesicle Picker enables automatic identification of vesicles in cryo-EM micrographs&lt;br /&gt;
with high recall and precision. It then exhaustively selects all potential particle locations, either at the perimeter&lt;br /&gt;
or uniformly over the surface of the projection of the vesicle. The program is designed to interface with cryoSPARC,&lt;br /&gt;
which performs both upstream micrograph processing and downstream single particle image analysis.&lt;br /&gt;
We demonstrate Vesicle Picker’s utility by determining a high-resolution map of the vacuolar-type ATPase from&lt;br /&gt;
micrographs of native synaptic vesicles (SVs) and identifying an additional protein or protein complex in the SV&lt;br /&gt;
membrane.&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/S1047847724000881&lt;br /&gt;
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== 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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