Abstract
Cross-linking/mass spectrometry (XL-MS) has come a long way. Originally, XL-MS was used to study relatively small, purified proteins. Meanwhile, it is employed to investigate protein-protein interactions on a proteome-wide level, giving snapshots of cellular processes. Currently, XL-MS is at the intersection of a multitude of workflows and the impact this technique has in addressing specific biological questions is steadily growing. This article is intended to give a bird’s-eye view of the current status of XL-MS, the benefits of using MS-cleavable cross-linkers, and the challenges posed in the future development of this powerful technology. We also illustrate how XL-MS can deliver valuable structural insights into protein complexes when used in combination with other structural techniques, such as electron microscopy.Graphical abstract
Highlights
Cross-linking/mass spectrometry (XL-MS) has come a long way
Since 2015, the number of annual publications for XL-MS has been leveling at ca. 350 (Fig. 1)
XL-MS is being increasingly used to determine protein-protein interaction networks at the system-wide level, delivering unprecedented insights compared to other methods, while at the same time requiring minimal amounts of sample
Summary
Apolipoprotein A-I Azide-tagged, acid-cleavable disuccinimidyl bissulfoxide Bis(sulfosuccinimidyl)suberate 4-{3-[3-(2,5-Dioxopyrrolidine-1-yloxycarbonyl) -propyl]-ureido}-butyric acid 2,5-dioxo-pyrrolidine-1-yl ester Cyanurbiotindipropionyl succinimide Collision-induced dissociation 1,4-Bis{4-[(2,5-dioxo-1-pyrrolidinyl) oxy]-4-oxobutyl}1,4-diazoniabicyclo[2.2.2]octane Disuccinimidyldibutyric urea Disuccinimidylsuberate Disuccinimidyl sulfoxide Electron microscopy. Published in the topical collection featuring Female Role Models in Analytical Chemistry
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
