| Literature DB >> 28114288 |
Michiel van de Waterbeemd1,2, Kyle L Fort1,2, Dmitriy Boll3, Maria Reinhardt-Szyba3, Andrew Routh4,5, Alexander Makarov1,3, Albert J R Heck1,2.
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.Entities:
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Year: 2017 PMID： 28114288 DOI： 10.1038/nmeth.4147
Source DB: PubMed Journal: Nat Methods ISSN： 1548-7091 Impact factor: 28.547