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

doi:10.1038/nmeth.4147

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

135 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 language	English (US)
Pages (from-to)	283-286
Number of pages	4
Journal	Nature Methods
Volume	14
Issue number	3
DOIs	https://doi.org/10.1038/nmeth.4147
State	Published - Feb 28 2017

ASJC Scopus subject areas

Biotechnology
Biochemistry
Molecular Biology
Cell Biology

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10.1038/nmeth.4147

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AU - Van De Waterbeemd, Michiel

AU - Fort, Kyle L.

AU - Boll, Dmitriy

AU - Reinhardt-Szyba, Maria

AU - Routh, Andrew

AU - Makarov, Alexander

AU - Heck, Albert J.R.

PY - 2017/2/28

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AB - 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.

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UR - https://www.scopus.com/pages/publications/85010867728#tab=citedBy

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JO - Nature Methods

JF - Nature Methods

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High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

Abstract

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