High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

Michiel Van De Waterbeemd, Kyle L. Fort, Dmitriy Boll, Maria Reinhardt-Szyba, Andrew Routh, Alexander Makarov, Albert J.R. Heck

Research output: Contribution to journalArticle

61 Scopus citations

Abstract

Investigation of the structure, assembly and function of protein-nucleic acid macromolecular machines requires multidimensional molecular and structural biology approaches. We describe modifications to an Orbitrap mass spectrometer, enabling high-resolution native MS analysis of 0.8-to 2.3-MDa prokaryotic 30S, 50S and 70S ribosome particles and the 9-MDa Flock House virus. The instrument's improved mass range and sensitivity readily exposes unexpected binding of the ribosome-associated protein SRA.

Original languageEnglish (US)
Pages (from-to)283-286
Number of pages4
JournalNature Methods
Volume14
Issue number3
DOIs
StatePublished - Feb 28 2017

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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  • Cite this

    Van De Waterbeemd, M., Fort, K. L., Boll, D., Reinhardt-Szyba, M., Routh, A., Makarov, A., & Heck, A. J. R. (2017). High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles. Nature Methods, 14(3), 283-286. https://doi.org/10.1038/nmeth.4147