Improved methods for building protein models in electron density maps and the location of errors in these models
T. Alwyn Jones, Jin-yu Zou, Sandra W. Cowan, Morten Kjeldgaard
Acta Crystallographica Section A Foundations of Crystallography · 1991 · 12,688 citations
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.
Cite this paper
Jones, T. A., Zou, J.- yu, Cowan, S. W., & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallographica Section A Foundations of Crystallography, 47(2), 110–119. https://doi.org/10.1107/s0108767390010224
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