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

Author

Listed:
  • 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
    St Petersburg Polytechnic University, Polytechnicheskaya, 29, 195251 St Petersburg, Russia
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • 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
    Institute of Microbiology and Genetics, Georg-August Universität, 37077 Göttingen, Germany)

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.

Suggested Citation

  • Niels Fischer & Piotr Neumann & Andrey L. Konevega & Lars V. Bock & Ralf Ficner & Marina V. Rodnina & Holger Stark, 2015. "Structure of the E. coli ribosome–EF-Tu complex at," Nature, Nature, vol. 520(7548), pages 567-570, April.
    • Handle: RePEc:nat:nature:v:520:y:2015:i:7548:d:10.1038_nature14275
    DOI: 10.1038/nature14275
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