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Science 4 November 2005:
Vol. 310. no. 5749, pp. 793 - 795
DOI: 10.1126/science.1120539

Perspectives

STRUCTURAL BIOLOGY:
A Ribosomal Coup: E. coli at Last!

Peter B. Moore

In his Perspective, Moore discusses the atomic-resolution structure that has been obtained by Schuwirth et al. for the Escherichia coli ribosome, the enzyme responsible for protein synthesis in that organism. The vast body of biochemical and genetic data obtained for this particle over the past half century can now be interpreted structurally.


The author is in the Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA. E-mail: peter.moore{at}yale.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site.
A. B. Taylor, B. Meyer, B. Z. Leal, P. Kotter, V. Schirf, B. Demeler, P. J. Hart, K.-D. Entian, and J. Wohnert (2008)
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Nucleolar Binding Sequences of the Ribosomal Protein S6e Family Reside in Evolutionary Highly Conserved Peptide Clusters.
S. Kundu-Michalik, M.-A. Bisotti, E. Lipsius, A. Bauche, A. Kruppa, T. Klokow, G. Kammler, and J. Kruppa (2008)
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Structural and evolutionary classification of G/U wobble basepairs in the ribosome.
A. Mokdad, M. V. Krasovska, J. Sponer, and N. B. Leontis (2006)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)