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Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. sect (1991)
| Venue: | A |
| Citations: | 1049 - 9 self |
BibTeX
@ARTICLE{Jones91improvedmethods,
author = {T. A. Jones and J. -y. Zou and S. W. Cowan and M. Kjeldgaard},
title = {Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. sect},
journal = {A},
year = {1991},
pages = {110--119}
}
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Abstract
Map interpretation remains a critical step in solving the structure of a macromolecule. Errors introduced at this early stage may persist throughout crystallo-graphic refinement and result in an incorrect struc-ture. 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 pep-tide and side-chain conformations.
