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.
Keywords
ResidualModel buildingBasis (linear algebra)Computer scienceInterpretation (philosophy)AlgorithmProcess (computing)Statistical physicsBiological systemCrystallographyMathematicsChemistryGeometryPhysicsBiology
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Publication Info
- Year
- 1991
- Type
- article
- Volume
- 47
- Issue
- 2
- Pages
- 110-119
- Citations
- 12647
- Access
- Closed
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Cite This
T. Alwyn Jones,
Jin-yu Zou,
Sandra W. Cowan
et al.
(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
Identifiers
- DOI
- 10.1107/s0108767390010224