Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 1, Pages 20-32Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2015.10.008
Keywords
-
Categories
Funding
- European Union 7th Framework Program (PROSPECTS) [HEALTH-F4-2008-201648]
- European Research Council (ERC Advanced Grants) [233226, 670821]
- Innovative Medicines Initiative Joint Undertaking (ULTRA-DD) [115366]
- European Molecular Biology Organization (EMBO)
Ask authors/readers for more resources
In recent years, chemical crosslinking of protein complexes and the identification of crosslinked residues by mass spectrometry (XL-MS; sometimes abbreviated as CX-MS) has become an important technique bridging mass spectrometry (MS) and structural biology. By now, XL-MS is well established and supported by publicly available resources as a convenient and versatile part of the structural biologist's toolbox. The combination of XL-MS with cryo-electron microscopy (cryo-EM) and/or integrative modeling is particularly promising to study the topology and structure of large protein assemblies. Among the targets studied so far are proteasomes, ribosomes, polymerases, chromatin remodelers, and photosystem complexes. Here we provide an overview of recent advances in XL-MS, the current state of the field, and a cursory outlook on future challenges.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available