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. 2017 Mar;14(3):283-286.
doi: 10.1038/nmeth.4147. Epub 2017 Jan 23.

High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

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High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

Michiel van de Waterbeemd et al. Nat Methods. 2017 Mar.

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.

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