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

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

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
Pages (from-to)	283-286
Number of pages	4
Journal	Nature Methods
Volume	14
DOIs	https://doi.org/10.1038/nmeth.4147
Publication status	Published - 23 Jan 2017

Keywords

Analytical biochemistry
Mass spectrometry
Proteins
Structure determination

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10.1038/nmeth.4147

10.1038nmeth.4147 2017 van de WaterbeemdAccepted author manuscript, 2.91 MB

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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.",

keywords = "Analytical biochemistry, Mass spectrometry, Proteins, Structure determination",

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T1 - High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

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 - 2017/1/23

Y1 - 2017/1/23

N2 - 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.

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.

KW - Analytical biochemistry

KW - Mass spectrometry

KW - Proteins

KW - Structure determination

U2 - 10.1038/nmeth.4147

DO - 10.1038/nmeth.4147

M3 - Article

C2 - 28114288

SN - 1548-7091

VL - 14

SP - 283

EP - 286

JO - Nature Methods

JF - Nature Methods

ER -

High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

Abstract

Keywords

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