Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures

Alexander Wlodawer, Wladek Minor, Zbigniew Dauter, Mariusz Jaskolski

Research output: Contribution to journalReview articlepeer-review

191 Scopus citations

Abstract

The number of macromolecular structures deposited in the Protein Data Bank now exceeds 45 000, with the vast majority determined using crystallographic methods. Thousands of studies describing such structures have been published in the scientific literature, and 14 Nobel prizes in chemistry or medicine have been awarded to protein crystallographers. As important as these structures are for understanding the processes that take place in living organisms and also for practical applications such as drug design, many non-crystallographers still have problems with critical evaluation of the structural literature data. This review attempts to provide a brief outline of technical aspects of crystallography and to explain the meaning of some parameters that should be evaluated by users of macromolecular structures in order to interpret, but not over-interpret, the information present in the coordinate files and in their description. A discussion of the extent of the information that can be gleaned from the coordinates of structures solved at different resolution, as well as problems and pitfalls encountered in structure determination and interpretation are also covered.

Original languageEnglish
Pages (from-to)1-21
Number of pages21
JournalFEBS Journal
Volume275
Issue number1
DOIs
StatePublished - Jan 2008
Externally publishedYes

Keywords

  • Protein Data Bank
  • Protein crystallography
  • R-factor
  • Resolution
  • Restraints
  • Structure determination
  • Structure interpretation
  • Structure quality
  • Structure refinement
  • Structure validation

Fingerprint

Dive into the research topics of 'Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures'. Together they form a unique fingerprint.

Cite this