Anomalous signal indicators in protein crystallography

Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1437-48. doi: 10.1107/S0907444905023589. Epub 2005 Oct 19.


A Monte Carlo procedure is described that generates random structure factors with simulated errors corresponding to an X-ray data set of a protein of a specific size and given heavy-atom content. The simulated data set can be used to estimate Bijvoet ratios and figures of merit as obtained from SAD phasing routines and can be used to gauge the feasibility of solving a structure via the SAD method. In addition to being able to estimate results from phasing, the simulation allows the estimation of the correlation coefficient between |DeltaF|, the absolute Bijvoet amplitude difference, and FA, the structure-factor amplitude of the heavy-atom model. As this quantity is used in various substructure-solution routines, the estimate provides a rough estimate of the ease of substructure solution. Furthermore, the Monte Carlo procedure provides an easy way of estimating the number of significant Bijvoet intensity differences, denoted as the measurability, and is proposed as an intuitive measure of the quality of anomalous data.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Computer Simulation
  • Crystallography, X-Ray / methods*
  • Fatty Acid Synthases / chemistry
  • Monte Carlo Method
  • Proteins / chemistry*
  • Thiolester Hydrolases / chemistry


  • Proteins
  • Fatty Acid Synthases
  • Thiolester Hydrolases
  • thioesterase II