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Research Article

Combined-information protein structure refinement: Potential energy-constrained real-space method for refinement with limited diffraction data

Susan Fitzwater and Harold A. Scheraga
PNAS March 1, 1982 79 (6) 2133-2137; https://doi.org/10.1073/pnas.79.6.2133
Susan Fitzwater
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Harold A. Scheraga
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Abstract

A potential energy-constrained real-space refinement method designed for use with x-ray diffraction data of low to moderate resolution has been developed. The number of adjustable parameters is severely restricted to ensure a reasonable ratio of data to parameters. Only dihedral angles are allowed to vary; bond lengths and bond angles are fixed at physically reasonable values. The structure of bovine pancreatic trypsin inhibitor was refined by using this method with data to only 2.5-Å resolution. Both the R-factor and the electron-density map improved throughout the refinement, and the final structure was a satisfactory approximation to the 1.5-Å structure.

  • UNICEPP potential energy function
  • bovine pancreatic trypsin inhibitor
  • x-ray diffraction data
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Combined-information protein structure refinement: Potential energy-constrained real-space method for refinement with limited diffraction data
Susan Fitzwater, Harold A. Scheraga
Proceedings of the National Academy of Sciences Mar 1982, 79 (6) 2133-2137; DOI: 10.1073/pnas.79.6.2133

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Combined-information protein structure refinement: Potential energy-constrained real-space method for refinement with limited diffraction data
Susan Fitzwater, Harold A. Scheraga
Proceedings of the National Academy of Sciences Mar 1982, 79 (6) 2133-2137; DOI: 10.1073/pnas.79.6.2133
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