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  Bayesian inference of rotor ring stoichiometry from electron microscopy images of archaeal ATP synthase

Cossio, P., Allegretti, M., Mayer, F., Müller, V., Vonck, J., & Hummer, G. (2018). Bayesian inference of rotor ring stoichiometry from electron microscopy images of archaeal ATP synthase. Microscopy, 67(5), 266-273. doi:10.1093/jmicro/dfy033.

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 Creators:
Cossio, Pilar1, 2, Author              
Allegretti, Matteo3, Author              
Mayer, Florian4, Author
Müller, Volker4, Author
Vonck, Janet3, Author              
Hummer, Gerhard1, 5, Author              
Affiliations:
1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
2Biophysics of Tropical Diseases, Max Planck Tandem Group, University of Antioquia, Medellín, Colombia, ou_persistent22              
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
4Department of Molecular Microbiology & Bioenergetics, Goethe University Frankfurt, Max-von-Laue-Strasse 9, Frankfurt am Main, Germany, ou_persistent22              
5Department of Physics, Goethe University Frankfurt, Max-von-Laue-Strasse 9, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: cryo-EM; symmetry; coarse-grained modeling; model comparison; likelihood analysis; BioEM
 Abstract: The ‘Bayesian inference of electron microscopy’ (BioEM) framework makes it possible to determine the stoichiometry of protein complexes using 3D coarse-grained models and a relatively small number of cryo-electron microscopy images as input. We applied the method to determine the most probable rotor ring stoichiometry of the archaeal Na+ ATP synthase from Pyrococcus furiosus, a multisubunit complex able to produce ATP under extreme conditions. Archaeal ATP synthases consist of a catalytic A1 part and a membrane-embedded AO portion. The AO portion is composed of a rotor ring and the a-subunit. The rotor ring of P. furiosus ATP synthase is composed of 16-kDa c-subunits, each consisting of four helices forming a bundle, with only one Na+-binding site per bundle. This ring was proposed to be decameric from LILBID-MS analysis of the entire ATP synthase. By contrast, the BioEM posterior favors a c9 ring stoichiometry. With BioEM, we ranked coarse-grained models of the whole complex with different ring geometry, using 6400 unprocessed particle images of the A1AO complex collected in vitreous ice. BioEM makes it possible to probabilistically establish the domain stoichiometry using low-resolution information and comparably few particle images.

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Language(s): eng - English
 Dates: 2017-12-192018-06-202018-07-192018-10-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1093/jmicro/dfy033
 Degree: -

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Title: Microscopy
  Other : Journal of Electron Microscopy
Source Genre: Journal
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Publ. Info: Oxford, UK : Oxford University Press
Pages: - Volume / Issue: 67 (5) Sequence Number: - Start / End Page: 266 - 273 Identifier: ISSN: 2050-5698
CoNE: https://pure.mpg.de/cone/journals/resource/2050-5698