Structural Mass Spectrometry of Protein Assemblies


In theory:

Cross-linking is now commonly used for structural purposes. Briefly, a cross-linker is used to link reactive amino-acids that are close together. After proteolytic digestion, the cross-linked peptides can be enriched (ion-exchange, SEC, biotinylated cross-linkers) and analysed by LC-MSMS. The distance restraints obtained by localizing the cross-linked residues can be used as an input to refine structural models.

In Practice:

We are currently implementing cross-linking MS at the IPBS on our orbitraps.



Chabrol E, Thépaut M, Dezutter-Dambuyant C, Vivès C, Marcoux J, Kahn R, Valadeau J, Vachette P, Durand D, Fieschi F (2015) “Alteration of the Langerin oligomerisation state affects Birbeck Granule formation” Biophysical Journal 108(3) : 666-677.


Marcoux J, Politis A, Marshall D, Rinehart D, Wallace MI, Tamm LK, Robinson CV (2014) “A new model for full length OmpA: native mass spectrometry reveals partial dimerization via C-ter domain” Structure 22(5) : 781-790.


Rozbeský D, Sovová Z, Marcoux J, Man P, Ettrich R, Robinson CV, Novák P (2013) “Structural model of lymphocyte receptor NKR-P1C revealed by mass spectrometry and molecular modelling” Analytical Chemistry 85(3) : 1597-604.