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Validation of protein crystal structures.

G J Kleywegt1

  • 1Department of Cell Biology, Uppsala University, Biomedical Centre, Box 596, SE-751 24 Uppsala, Sweden. gerard@xray.bmc.uu.se

Acta Crystallographica. Section D, Biological Crystallography
|March 14, 2000
PubMed
Summary

Quality control is essential for validating biomacromolecular models derived from crystallographic data. This review compiles methods and lessons learned for assessing the accuracy of protein crystal structures.

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Crystallography

Background:

  • Macromolecular modeling from crystallographic data involves subjective interpretation.
  • Robust quality control is crucial for ensuring the reliability of these models.
  • The 1990s saw significant advancements in validation methodologies.

Purpose of the Study:

  • To review quality-control techniques for biomacromolecular models.
  • To share lessons learned in model refinement and validation.
  • To compile a comprehensive compendium of validation criteria and methods.

Main Methods:

  • Review of historical data and methodologies from the 1990s.
  • Compilation of existing and historical quality-control criteria.
  • Focus on methods applicable to protein crystal structure validation.

Main Results:

  • Identification of key quality-control techniques and their evolution.
  • Documentation of challenges and successes in biomacromolecular model validation.
  • A structured compendium of validation approaches.

Conclusions:

  • Subjectivity in model building necessitates rigorous quality assessment.
  • Continuous development and application of validation methods are vital.
  • Standardized quality control enhances the reliability of protein structure models.

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