Chapter 21.1 Validation of protein crystal structures
Published Online: 1 JAN 2006
© International Union of Crystallography 2006
International Tables for Crystallography
How to Cite
Kleywegt, G. J. 2006. Validation of protein crystal structures. International Tables for Crystallography. F:497–506.
- Published Online: 1 JAN 2006
Since the process of building and refining a model of a biomacromolecule based on crystallographic data is subjective, quality-control techniques are required to assess the validity of such models. During the 1990s, much experience was gained; the methods used and some of the lessons learned are reviewed here. In addition, an extensive compendium of quality criteria and quality-control methods that are or have been used to validate models of biomacromolecules has been compiled. The emphasis in this compendium is on the validation of protein crystal structures.
Keywords: accuracy; atomic displacement parameters (temperature factors); Calpha-only model; coordinate errors; data completeness; data resolution; difference density quality; errors; merging R factors; noncrystallographic symmetry; outliers; quality indicators; real-space fit; signal strength and structure validation; solvent; structure validation; temperature factors (atomic displacement parameters); unit-cell parameters