4.8 Article

High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

Journal

NATURE METHODS
Volume 14, Issue 3, Pages 283-+

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.4147

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Funding

  1. Netherlands Organization for Scientific Research (NWO)
  2. Fundamenteel Onderzoek der Materie (FOM) [12PR3303-2]
  3. European Union [686547]
  4. University of Texas Medical Branch (UTMB) startup fund
  5. Texas Rising STARs Award from the University of Texas System
  6. Netherlands Proteomics Centre [184.032.201]

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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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