Blog
About

68
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      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

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

      Read this article at

      ScienceOpenPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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.

          Related collections

          Author and article information

          Journal
          2025413

          Comments

          Comment on this article