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Journal Article

Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM.

MPS-Authors
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Fischer,  N.
Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society;

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Konevega,  A. L.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Bock,  L. V.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Stark,  H.
Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

2104845.pdf
(Publisher version), 7MB

Supplementary Material (public)

2104845_Suppl_1.html
(Supplementary material), 93KB

2104845_Suppl_2.html
(Supplementary material), 95KB

Citation

Fischer, N., Neumann, P., Konevega, A. L., Bock, L. V., Ficner, R., Rodnina, M. V., et al. (2015). Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM. Nature, 520(7548), 567-570. doi:10.1038/nature14275.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0025-023D-E
Abstract
Single particle electron cryomicroscopy (cryo-EM) has recently made significant progress in high-resolution structure determination of macromolecular complexes due to improvements in electron microscopic instrumentation and computational image analysis. However, cryo-EM structures can be highly non-uniform in local resolution1, 2 and all structures available to date have been limited to resolutions above 3 Å3, 4. Here we present the cryo-EM structure of the 70S ribosome from Escherichia coli in complex with elongation factor Tu, aminoacyl-tRNA and the antibiotic kirromycin at 2.65–2.9 Å resolution using spherical aberration (Cs)-corrected cryo-EM. Overall, the cryo-EM reconstruction at 2.9 Å resolution is comparable to the best-resolved X-ray structure of the E. coli 70S ribosome5 (2.8 Å), but provides more detailed information (2.65 Å) at the functionally important ribosomal core. The cryo-EM map elucidates for the first time the structure of all 35 rRNA modifications in the bacterial ribosome, explaining their roles in fine-tuning ribosome structure and function and modulating the action of antibiotics. We also obtained atomic models for flexible parts of the ribosome such as ribosomal proteins L9 and L31. The refined cryo-EM-based model presents the currently most complete high-resolution structure of the E. coli ribosome, which demonstrates the power of cryo-EM in structure determination of large and dynamic macromolecular complexes.