The 1.25 Å resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site
- 1 October 1998
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 282 (5) , 1043-1059
- https://doi.org/10.1006/jmbi.1998.2076
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Who checks the checkers? four validation tools applied to eight atomic resolution structuresJournal of Molecular Biology, 1998
- The benefits of atomic resolutionCurrent Opinion in Structural Biology, 1997
- Improved R-factors for diffraction data analysis in macromolecular crystallographyNature Structural & Molecular Biology, 1997
- The structure of concanavalin A and its bound solvent determined with small-molecule accuracy at 0.94 [Aring ]resolutionJournal of the Chemical Society, Faraday Transactions, 1997
- High Resolution Crystal Structures of the Deoxy, Oxy, and Aquomet Forms of Cobalt MyoglobinPublished by Elsevier ,1996
- Delineation and comparison of ganglioside-binding epitopes for the toxins of Vibrio cholerae, Escherichia coli, and Clostridium tetani: evidence for overlapping epitopes.Proceedings of the National Academy of Sciences, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Accurate bond and angle parameters for X-ray protein structure refinementActa Crystallographica Section A Foundations of Crystallography, 1991
- General definition of ring puckering coordinatesJournal of the American Chemical Society, 1975