Chapter 18.4 Refinement at atomic resolution

Crystallography of biological macromolecules

First Online Edition (2006)

Part 18. Refinement

  1. Z. Dauter1,
  2. G. N. Murshudov2,
  3. K. S. Wilson3

Published Online: 1 JAN 2006

DOI: 10.1107/97809553602060000696

International Tables for Crystallography

International Tables for Crystallography

How to Cite

Dauter, Z., Murshudov, G. N. and Wilson, K. S. 2006. Refinement at atomic resolution. International Tables for Crystallography. F:18:18.4:393–402.

Author Information

  1. 1

    National Cancer Institute, Brookhaven National Laboratory, Building 725A-X9, Upton, NY 11973, USA

  2. 2

    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England, and CLRC, Daresbury Laboratory, Daresbury, Warrington, WA4 4AD, England

  3. 3

    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England

Publication History

  1. Published Online: 1 JAN 2006


The first part of this chapter gives a definition of atomic resolution. This is followed by a discussion of data quality and anisotropic scaling of data. Computational algorithms and strategies are then covered as are computational options and tactics. Those features of the refined model that are especially enhanced in an atomic resolution analysis are described. Finally, the biological issues that are addressed by analysis of macromolecular structures at atomic resolution are discussed.


  • ab initio phasing;
  • alternative conformations;
  • anisotropic scaling;
  • atomic displacement parameters;
  • atomic resolution;
  • automatic location of water sites;
  • bulk solvent modelling;
  • constraints;
  • deformation density;
  • fast Fourier transform;
  • least-squares methods;
  • ligands at atomic resolution;
  • maximum likelihood;
  • metal ions at atomic resolution;
  • partial occupancy;
  • phasing;
  • refinement;
  • restraints;
  • scaling;
  • solvent