On the evolution of the quality of macromolecular models in the PDB

FEBS J. 2020 Jul;287(13):2685-2698. doi: 10.1111/febs.15314. Epub 2020 Apr 20.

Abstract

Crystallographic models of biological macromolecules have been ranked using the quality criteria associated with them in the Protein Data Bank (PDB). The outcomes of this quality analysis have been correlated with time and with the journals that published papers based on those models. The results show that the overall quality of PDB structures has substantially improved over the last ten years, but this period of progress was preceded by several years of stagnation or even depression. Moreover, the study shows that the historically observed negative correlation between journal impact and the quality of structural models presented therein seems to disappear as time progresses.

Keywords: PDB; X-ray crystallography; nucleic acids; proteins; structure quality.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Computational Biology / methods*
  • Databases, Protein / standards*
  • Macromolecular Substances / chemistry*
  • Models, Molecular*
  • Protein Conformation
  • Protein Domains
  • Proteins / chemistry*
  • Quality Control*

Substances

  • Macromolecular Substances
  • Proteins