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

Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M.·1991·Acta Crystallographica Section A Foundations of Crystallography

DOI 10.1107/s0108767390010224

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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 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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Untitled work
(1999) · doi:10.1002/(sici)1097-0134(1999)37:3+<171::aid-prot21>3.0.co;2-z

Authors: Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M.
Venue: Acta Crystallographica Section A Foundations of Crystallography
Publisher: International Union of Crystallography (IUCr)
Published: 1991-03-01
Volume: 47
Issue: 2
Pages: 110-119
ISSN: 0108-7673 (ISSN-L)
DOI: 10.1107/s0108767390010224
OpenAlex: W2013083986
Cited by: 12,648
References: 0
FWCI: 106.34
Type: journal article
Language: en
Open access: closed

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

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