Dataset Information

Reliable identification of protein-protein interactions by crosslinking mass spectrometry_Protein coelution

ABSTRACT: Quantitative proteomics dataset on soluble, SEC-fractionated high-molecular weight proteome of E. coli for protein coelution analysis. This data was used to identify proteins for a subsequent crosslinking mass spectrometry search (DB creation) and to correlate protein elution behaviour to validate/falsify potential PPIs from the CLMS-based approach. Cleared E. coli lysate was fractionated in the range of 3 MDa to 150 kDa (44 fractions). The proteins in each fraction were precipitated, derivatized and proteolysed in-solution. Then, each fraction was acquired via LC-MS on Q Exactive HF and the raw data searched with MaxQuant with iBAQ quantitation enabled.

ORGANISM(S): Escherichia Coli

SUBMITTER: Prof. Dr. Juri Rappsilber

PROVIDER: PXD019004 | JPOST Repository | Wed Apr 14 00:00:00 BST 2021

REPOSITORIES: jPOST

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Dataset's files

Source:

			Action	DRS
	B181215_26_HF_LS_IN_90_ECLP_ID_24.raw	Raw
	B181215_27_HF_LS_IN_90_ECLP_ID_23.raw	Raw
	B181215_28_HF_LS_IN_90_ECLP_ID_22.raw	Raw
	B181215_29_HF_LS_IN_90_ECLP_ID_21.raw	Raw
	B181215_30_HF_LS_IN_90_ECLP_ID_20.raw	Raw

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Reliable identification of protein-protein interactions by crosslinking mass spectrometry.

Lenz Swantje S Sinn Ludwig R LR O'Reilly Francis J FJ Fischer Lutz L Wegner Fritz F Rappsilber Juri J

Nature communications 20210611 1

Protein-protein interactions govern most cellular pathways and processes, and multiple technologies have emerged to systematically map them. Assessing the error of interaction networks has been a challenge. Crosslinking mass spectrometry is currently widening its scope from structural analyses of purified multi-protein complexes towards systems-wide analyses of protein-protein interactions (PPIs). Using a carefully controlled large-scale analysis of Escherichia coli cell lysate, we demonstrate t ...[more]

PMID: 34117231

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