Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Matteo Allegretti, Niklas Klusch, Deryck J. Mills, Janet Vonck, Werner Kühlbrandt () and Karen M. Davies ()
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Matteo Allegretti: Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany
Niklas Klusch: Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany
Deryck J. Mills: Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany
Janet Vonck: Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany
Werner Kühlbrandt: Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany
Karen M. Davies: Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany

Nature, 2015, vol. 521, issue 7551, 237-240

Abstract: Electron cryomicroscopy of a complete mitochondrial ATP-synthase dimer reveals the elusive structure of the essential a-subunit.

Date: 2015
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DOI: 10.1038/nature14185

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