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

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

T A Jones  1 , J Y Zou, S W Cowan, M Kjeldgaard
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Improved methods for building protein models in electron density maps and the location of errors in these models

T A Jones et al. Acta Crystallogr A. .

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.

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