Nature 407, 327-339 (21 September 2000) | doi:10.1038/35030006; Received 14 July 2000; Accepted 10 August 2000

Structure of the 30S ribosomal subunit

Brian T. Wimberly1,2, Ditlev E. Brodersen1,2, William M. Clemons, Jr1,2,3, Robert J. Morgan-Warren1,2, Andrew P. Carter1,2, Clemens Vonrhein4, Thomas Hartsch5 & V. Ramakrishnan2

  1. MRC Laboratory of Molecular Biology , Hills Road, Cambridge CB2 2QH, UK
  2. Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84132, USA
  3. Global Phasing Ltd., Sheraton House , Castle Park, Cambridge CB3 0AX, UK
  4. Göttingen Genomics Laboratory, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany
  5. These authors contributed equally to this work

Correspondence to: V. Ramakrishnan2 Correspondence and requests for materials should be addressed to V.R. (e-mail: Email: Coordinates have been deposited in the Protein Data Bank, accession number 1FJF. Coordinates of individual components will be made available on


Genetic information encoded in messenger RNA is translated into protein by the ribosome, which is a large nucleoprotein complex comprising two subunits, denoted 30S and 50S in bacteria. Here we report the crystal structure of the 30S subunit from Thermus thermophilus, refined to 3 Å resolution. The final atomic model rationalizes over four decades of biochemical data on the ribosome, and provides a wealth of information about RNA and protein structure, protein–RNA interactions and ribosome assembly. It is also a structural basis for analysis of the functions of the 30S subunit, such as decoding, and for understanding the action of antibiotics. The structure will facilitate the interpretation in molecular terms of lower resolution structural data on several functional states of the ribosome from electron microscopy and crystallography.