Cross-linking mass spectrometry for mapping protein complex topologies in situ

5Citations
Citations of this article
25Readers
Mendeley users who have this article in their library.

Abstract

Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study the structure of protein complexes in situ, such as in organelles, cells, and even tissues, is still a technological frontier. The complexity of these systems remains a considerable challenge, but there have been dramatic improvements in sample handling, data acquisition, and data processing. Here, we summarise these developments and describe the paths towards comprehensive and comparative structural interactomes by cross-linking mass spectrometry.

Cite

CITATION STYLE

APA

Lee, K., & O’Reilly, F. J. (2023, March 1). Cross-linking mass spectrometry for mapping protein complex topologies in situ. Essays in Biochemistry. Portland Press Ltd. https://doi.org/10.1042/EBC20220168

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free