Structural analysis of protein complexes by cross-linking and mass spectrometry

Moriya Slavin, Nir Kalisman*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

9 Scopus citations

Abstract

Cross-linking and mass spectrometry is used more and more for the structural analysis of large proteins and protein complexes. Although essentially a low-resolution method, it avoids the main drawbacks of established structural techniques. Particularly, it is largely insensitive to the inherent flexibility of the studied complexes and is applied under native conditions. It is also applicable to nearly every structural system. Therefore, cross-linking and mass spectrometry is the method of choice for elucidating the general architecture of protein complexes. Advances in instrumentation, techniques, and software now allow every lab that is working with proteins to apply the approach without much difficulty. The most specialized step in the workflow, the mass spectrometry measurement, can be done in most facilities that are performing standard proteomics. We detail here a step-by-step protocol of how to successfully apply the approach in collaboration with the mass spectrometry facility in your institution.

Original languageAmerican English
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages173-183
Number of pages11
DOIs
StatePublished - 2018

Publication series

NameMethods in Molecular Biology
Volume1764
ISSN (Print)1064-3745

Bibliographical note

Publisher Copyright:
© 2018, Springer Science+Business Media, LLC, part of Springer Nature.

Keywords

  • Molecular machines
  • Protein architecture
  • Structural biology

Fingerprint

Dive into the research topics of 'Structural analysis of protein complexes by cross-linking and mass spectrometry'. Together they form a unique fingerprint.

Cite this