Chapter 18.4 Refinement at atomic resolution

Crystallography of biological macromolecules

Second Online Edition (2012)

Part 18. Refinement

  1. Z. Dauter1,
  2. G. N. Murshudov2,
  3. K. S. Wilson2

Published Online: 14 APR 2012

DOI: 10.1107/97809553602060000858

International Tables for Crystallography

International Tables for Crystallography

How to Cite

Dauter, Z., Murshudov, G. N. and Wilson, K. S. 2012. Refinement at atomic resolution. International Tables for Crystallography. F:18:18.4:485–498.

Author Information

  1. 1

    NCI Frederick & Argonne National Laboratory, Building 202, Argonne, IL 60439, USA

  2. 2

    York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, UK

Publication History

  1. Published Online: 14 APR 2012


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