Over the past decade, cross-linking mass spectrometry (CLMS) has developed into a robust
and flexible tool that provides medium-resolution structural information. CLMS data provide …

Structural mass spectrometry (MS) is gaining increasing importance for deriving valuable
three‐dimensional structural information on proteins and protein complexes, and it …

Crosslinking mass spectrometry has become a core technology in structural biology and is
expanding its reach towards systems biology. Its appeal lies in a rapid workflow, high …

Observing the structures of proteins within the cell and tracking structural changes under
different cellular conditions are the ultimate challenges for structural biology. This, however …

A major challenge in cross-linking/mass spectrometry (MS) is targeting carboxyl functions in
proteins under physiological conditions that do not disturb the protein's conformation. Cross …

For decades, chemical cross-linking of proteins has been an established method to study
protein interaction partners. The chemical cross-linking approach has recently been revived …

With the advance of experimental procedures obtaining chemical crosslinking information is
becoming a fast and routine practice. Information on crosslinks can greatly enhance the …

Cross-linking/mass spectrometry has undergone a maturation process akin to standard
proteomics by adapting key methods such as false discovery rate control and quantification …

Experimental data offers empowering constraints for structure prediction. These constraints
can be used to filter equivalently scored models or more powerfully within optimization …

Free radical‐initiated peptide sequencing (FRIPS) has recently been introduced as an
analytical strategy to create peptide radical ions in a predictable and effective way by …