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

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

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1
Department of Molecular Biology, BMC, Uppsala, Sweden.

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.

PMID:
2025413
[Indexed for MEDLINE]
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