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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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          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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          Author and article information

          Journal
          Acta Crystallogr A
          Acta crystallographica. Section A, Foundations of crystallography
          International Union of Crystallography (IUCr)
          0108-7673
          0108-7673
          Mar 01 1991
          : 47 ( Pt 2)
          Affiliations
          [1 ] Department of Molecular Biology, BMC, Uppsala, Sweden.
          Article
          10.1107/s0108767390010224
          2025413
          1b94f798-c660-4073-a089-2cbde0777727
          History

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