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      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
      Chemistry, Physical, Computer Graphics, Crystallization, Models, Molecular, Molecular Structure, Physicochemical Phenomena, Proteins, chemistry, Software, X-Ray Diffraction

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          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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