Structure of a bacterial 30S ribosomal subunit at 5.5 Å resolution

William M. Clemons, Joanna L. C. May, Brian T. Wimberly, John P. McCutcheon, Malcolm S. Capel and V. Ramakrishnan ()
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William M. Clemons: University of Utah School of Medicine
Joanna L. C. May: University of Utah School of Medicine
Brian T. Wimberly: University of Utah School of Medicine
John P. McCutcheon: University of Utah School of Medicine
Malcolm S. Capel: Brookhaven National Laboratory
V. Ramakrishnan: University of Utah School of Medicine

Nature, 1999, vol. 400, issue 6747, 833-840

Abstract: Abstract The 30S ribosomal subunit binds messenger RNA and the anticodon stem-loop of transfer RNA during protein synthesis. A crystallographic analysis of the structure of the subunit from the bacterium Thermus thermophilus is presented. At a resolution of 5.5 Å, the phosphate backbone of the ribosomal RNA is visible, as are the α-helices of the ribosomal proteins, enabling double-helical regions of RNA to be identified throughout the subunit, all seven of the small-subunit proteins of known crystal structure to be positioned in the electron density map, and the fold of the entire central domain of the small-subunit ribosomal RNA to be determined.

Date: 1999
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DOI: 10.1038/23631

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