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March 1, 1991Acta Crystallographica Section A Foundations of Crystallography12,690 citations

Improved methods for building protein models in electron density maps and the location of errors in these models

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TJT. Alwyn JonesJohns Hopkins UniversityJZJin-yu ZouUppsala UniversitySCSandra W. CowanAustralian National University

Key Points

  • To introduce computational strategies and tools that simplify macromolecular model building and accurately locate structural errors within electron density maps.
  • Designed algorithmic strategies to streamline the interpretation of electron density maps during macromolecular structure determination.
  • Implemented residue-level validation metrics to assess local goodness of fit and screen for conformational errors in peptide backbones and side chains.
  • Established per-residue evaluation criteria that overcome the diagnostic limitations of global crystallographic residuals.
  • Enabled targeted detection and correction of conformational errors in peptide and amino acid side chains prior to crystallographic refinement.

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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Cite This Study

Jones et al. (1991) studied this question.

synapsesocial.com/papers/69dd62000a7b4bc8c4101eb3https://doi.org/10.1107/s0108767390010224
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