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

Clemons, William M. Jr
May, Joanna L. C.
Wimberly, Brian T.
McCutcheon, John P.
Capel, Malcolm S.
Ramakrishnan, V.

(Clemons, May, Wimberly, McCutcheon, Ramakrishnan) Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84103, USA
(Capel) Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA
(Ramakrishnan) Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UK
(Clemons, May, Wimberly) These authors contributed equally to this work.

Nature 400(6747):p 833-840, August 26, 1999.

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 Angstrom, the phosphate backbone of the ribosomal RNA is visible, as are the alpha-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.