Journal
NATURE METHODS
Volume 11, Issue 4, Pages 403-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.2841
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Funding
- PROSPECTS (Proteomics Specification in Space and Time) within the European Union 7th Framework Program [HEALTH-F4-2008-201648]
- European Research Council [233226, 268851]
- Medical Research Council [G1000819]
- Wellcome Trust [095951]
- Royal Society
- MRC [G1000819] Funding Source: UKRI
- Medical Research Council [G1000819] Funding Source: researchfish
- European Research Council (ERC) [268851] Funding Source: European Research Council (ERC)
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We describe a method that integrates data derived from different mass spectrometry (MS)-based techniques with a modeling strategy for structural characterization of protein assemblies. We encoded structural data derived from native MS, bottom-up proteomics, ion mobility-MS and chemical cross-linking MS into modeling restraints to compute the most likely structure of a protein assembly. We used the method to generate near-native models for three known structures and characterized an assembly intermediate of the proteasomal base.
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