In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria

The field of structural biology is increasingly focusing on studying proteins in situ, i.e., in their greater biological context. Cross-linking mass spectrometry (CLMS) is contributing to this effort, typically through the use of mass spectrometry (MS)-cleavable cross-linkers. Here, we apply the pop...

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Bibliographic Details
Published in:	Journal of proteome research Vol. 19; no. 1; p. 327
Main Authors:	Ryl, Petra S J, Bohlke-Schneider, Michael, Lenz, Swantje, Fischer, Lutz, Budzinski, Lisa, Stuiver, Marchel, Mendes, Marta M L, Sinn, Ludwig, O'Reilly, Francis J, Rappsilber, Juri
Format:	Journal Article
Language:	English
Published:	United States 03.01.2020
Subjects:	Chromatography, Gel Cross-Linking Reagents - chemistry Humans K562 Cells Mass Spectrometry - methods Mitochondria - chemistry Mitochondrial Proteins - analysis Mitochondrial Proteins - chemistry Protein Conformation Protein Interaction Maps Succinimides - chemistry Workflow noncleavable DSS cross-linker in situ large-scale structural biology comparative modeling human mitochondria cross-linking mass spectrometry
ISSN:	1535-3907, 1535-3907
Online Access:	Get more information
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