Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

The 2- angstrom Resolution Structure of a Thermostable Ribonuclease A Chemically Cross-Linked between Lysine Residues 7 and 41

P. C. Weber, S. Sheriff, D. H. Ohlendorf, B. C. Finzel and F. R. Salemme
Proceedings of the National Academy of Sciences of the United States of America
Vol. 82, No. 24 (Dec. 15, 1985), pp. 8473-8477
Stable URL: http://www.jstor.org/stable/26611
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
The 2- angstrom Resolution Structure of a Thermostable Ribonuclease A Chemically Cross-Linked between Lysine Residues 7 and 41
Preview not available

Abstract

The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0- angstrom resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 angstrom, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.

Page Thumbnails

  • Thumbnail: Page 
8473
    8473
  • Thumbnail: Page 
8474
    8474
  • Thumbnail: Page 
8475
    8475
  • Thumbnail: Page 
8476
    8476
  • Thumbnail: Page 
8477
    8477