Comprehensive cross-linking mass spectrometry reveals molecular insights into the between peripheral and core NuRD complex subunits
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ABSTRACT: Affinity purifications of different subunits of the NuRD complex, followed by cross-linking mass spectrometry (xIP-MS) to identify interaction domains. Six subunits and an interactor of NuRD were cross-inked with either BS3 or ADH/DMTMM and digested with either trypsin or chymotrypsin, to generate a dense cross-link network.
INSTRUMENT(S): LTQ FT, LTQ Orbitrap Velos
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Permanent Cell Line Cell, Cell Culture
SUBMITTER: Cornelia Spruijt
LAB HEAD: Michiel Vermeulen
PROVIDER: PXD017244 | Pride | 2020-12-07
REPOSITORIES: Pride
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