Structure of the E. coli ribosome–EF-Tu complex at

Niels Fischer (), Piotr Neumann, Andrey L. Konevega, Lars V. Bock, Ralf Ficner, Marina V. Rodnina and Holger Stark ()
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Niels Fischer: 3D Electron Cryomicroscopy Group, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Piotr Neumann: Institut für Mikrobiologie und Genetik, GZMB, Georg-August Universität Göttingen, Justus-von Liebig Weg 11, 37077 Göttingen, Germany
Andrey L. Konevega: B.P. Konstantinov Petersburg Nuclear Physics Institute of National Research Centre ‘Kurchatov Institute’, 188300 Gatchina, Russia
Lars V. Bock: Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Ralf Ficner: Institut für Mikrobiologie und Genetik, GZMB, Georg-August Universität Göttingen, Justus-von Liebig Weg 11, 37077 Göttingen, Germany
Marina V. Rodnina: Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Holger Stark: 3D Electron Cryomicroscopy Group, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany

Nature, 2015, vol. 520, issue 7548, 567-570

Abstract: A single particle cryo-EM structure of the 70S ribosome in complex with the elongation factor Tu breaks the 3 Å resolution barrier of the technique and locally exceeds the resolution of previous crystallographic studies, revealing all modifications in rRNA and explaining their roles in ribosome function and antibiotic binding.

Date: 2015
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DOI: 10.1038/nature14275

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