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citation_title: Structure of the E. coli ribosome-EF-Tu complex at <3 A resolution by Cs-corrected cryo-EM
WT.cg_s: Letter
access: Yes
keywords: Cryoelectron microscopy, Ribosome, Bacterial structural biology, Cryoelectron microscopy
emanating: 134X76X223X157
citation_publisher: Nature Publishing Group
citation_journal_title: Nature
WT.tz: America/New_York
description: 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 resolution and all structures available to date have been limited to resolutions above 3 A. 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 A resolution using spherical aberration (Cs)-corrected cryo-EM. Overall, the cryo-EM reconstruction at 2.9 A resolution is comparable to the best-resolved X-ray structure of the E. coli 70S ribosome (2.8 A), but provides more detailed information (2.65 A) 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.
WT.site_id: 18696
citation_date: 
title: 
DC.title: Structure of the E. coli ribosome-EF-Tu complex at <3 A resolution by Cs-corrected cryo-EM
DC.date: 2015-02-23
prism.issn: 0028-0836
DC.publisher: Nature Publishing Group
citation_online_date: 2015-02-23
WT.cg_n: Nature
DC.creator: Niels Fischer
prism.issue: 
DC.identifier: doi:10.1038/nature14275
dc:title: 
Content-Encoding: UTF-8
prism.publicationDate: 2015-02-23
robots: noarchive
DC.rights: © 2015 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
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prism.rightsAgent: permissions@nature.com
citation_author: Niels Fischer
citation_issue: 
prism.eIssn: 1476-4687
DC.language: en
prism.volume: 
citation_firstpage: 
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WT.template: C
prism.publicationName: Nature
citation_doi: doi:10.1038/nature14275
prism.section: Letter
citation_volume: 
Content-Language: en
prism.copyright: © 2015 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.