In this study, we used bottom-up proteomics and cross-linking MS (XL-MS) to study the composition and structure of soluble membrane attack complex (sMAC). For bottom-up proteomics sMAC was digested using trypsin and analyzed on Orbitrap Fusion Lumos. For the cross-linking analysis sMAC was cross-linked using DMTMM or DSS. The cross-linked proteins were digested using trypsin and the data was acquired using an Ultimate 3000 system coupled on-line to an Orbitrap Fusion. Proteomics raw data was searched using MaxQuant and cross-linking raw data was searched using pLink.
[doi:10.25345/C5JF80]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Complement ; XL-MS ; Bottom-up
Principal Investigators: (in alphabetical order) |
Albert J.R. Heck, Biomolecular Mass Spectrometry and Proteomics groups, Utrecht University, N/A |
Submitting User: | M_Lukassen |
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