High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles
Publication date
2017-01-23
Authors
van de Waterbeemd, M.J.
Fort, Kyle L
Boll, Dmitriy
Reinhardt-Szyba, Maria
Routh, Andrew
Makarov, Alexander
Heck, Albert J R
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Document Type
Article
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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
Citation
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, vol. 14, pp. 283-286. https://doi.org/10.1038/nmeth.4147