IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v400y1999i6747d10.1038_23631.html
   My bibliography  Save this article

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

Author

Listed:
  • 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
    MRC Laboratory of Molecular Biology)

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.

Suggested Citation

  • William M. Clemons & Joanna L. C. May & Brian T. Wimberly & John P. McCutcheon & Malcolm S. Capel & V. Ramakrishnan, 1999. "Structure of a bacterial 30S ribosomal subunit at 5.5 Å resolution," Nature, Nature, vol. 400(6747), pages 833-840, August.
    • Handle: RePEc:nat:nature:v:400:y:1999:i:6747:d:10.1038_23631
    DOI: 10.1038/23631
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/23631
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/23631?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:400:y:1999:i:6747:d:10.1038_23631. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.