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  In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits

Mühleip, A. W., Dewar, C. E., Schnaufer, A., Kühlbrandt, W., & Davies, K. M. (2017). In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits. Proceedings of the National Academy of Sciences of the United States of America, 114(5), 992-997. doi:10.1073/pnas.1612386114.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-A131-5 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-A15F-5
Genre: Journal Article

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 Creators:
Mühleip, Alexander W.1, Author           
Dewar, Caroline E.2, Author
Schnaufer, Achim2, Author
Kühlbrandt, Werner1, Author                 
Davies, Karen M.1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Institute of Immunology and Infection Research and Centre for Immunity, Infection, and Evolution, University of Edinburgh, Edinburgh EH9 3FL, United Kingdom, ou_persistent22              

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Free keywords: mitochondrial ATP synthase, electron cryotomography, subtomogram, averaging, trypanosome, rotary catalysis
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Language(s): eng - English
 Dates: 2017
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1612386114
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 114 (5) Sequence Number: - Start / End Page: 992 - 997 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230