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Related Experiment Videos

Efficient rebuilding of protein structures.

G J Kleywegt1, T A Jones

  • 1Department of Molecular Biology, Biomedical Centre, Uppsala University, Sweden. gerard@xray.bmc.uu.se

Acta Crystallographica. Section D, Biological Crystallography
|July 1, 1996
PubMed
Summary
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The OOPS computer program aids in rebuilding protein structures within electron density maps, improving crystallographic model building. It identifies and flags unreasonable protein residues to prevent errors in structure determination.

Area of Science:

  • Structural Biology
  • Computational Biology
  • Crystallography

Background:

  • Protein structure determination is crucial for understanding biological function.
  • Crystallographic methods are widely used but can be prone to local errors during model building.
  • Accurate rebuilding of protein models within electron density is essential for reliable results.

Purpose of the Study:

  • To introduce a novel computer program, OOPS, designed to enhance protein structure rebuilding.
  • To reduce the propagation of local errors during crystallographic structure determination.
  • To assist crystallographers in identifying and correcting problematic residues in protein models.

Main Methods:

  • Development of the OOPS (Outlying Observation Protein Structure) computer program.

Related Experiment Videos

  • Implementation of criteria to assess the reasonableness of individual protein residues.
  • Generation of macros for the macromolecular crystallographic model-building program 'O'.

    • Main Results:

    • OOPS facilitates and accelerates the process of rebuilding protein structures.
    • The program effectively reduces the likelihood of local errors persisting in the final model.
    • OOPS guides users along suspect residues, aiding in error identification and correction.

    Conclusions:

    • OOPS is a valuable tool for improving the accuracy and efficiency of protein model rebuilding in crystallography.
    • The program contributes to more reliable protein structure determination by minimizing local errors.
    • OOPS enhances the workflow for crystallographers, particularly in identifying and resolving ambiguous regions of electron density.