Improved methods for building protein models in electron density maps and the location of errors in these models
Volume: 47, Issue: 2, Pages: 110 - 119
Published: Mar 1, 1991
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...
Paper Details
Title
Improved methods for building protein models in electron density maps and the location of errors in these models
Published Date
Mar 1, 1991
Volume
47
Issue
2
Pages
110 - 119
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