Improved methods for building protein models in electron density maps and the location of errors in these models

Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9. doi: 10.1107/s0108767390010224.

Abstract

Map interpretation remains a critical step in solving the structure of a macromolecule. Errors introduced at this early stage may persist throughout crystallographic refinement and result in an incorrect structure. The normally quoted crystallographic residual is often a poor description for the quality of the model. Strategies and tools are described that help to alleviate this problem. These simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • Computer Graphics
  • Crystallization
  • Models, Molecular*
  • Molecular Structure
  • Proteins / chemistry*
  • Software
  • X-Ray Diffraction

Substances

  • Proteins