Chapter

Chapter 4.3 Application of protein engineering to improve crystal properties

Crystallography of biological macromolecules

First Online Edition (2006)

Part 4. Crystallization

  1. D. R. Davies,
  2. A. Burgess Hickman

Published Online: 1 JAN 2006

DOI: 10.1107/97809553602060000662

International Tables for Crystallography

International Tables for Crystallography

How to Cite

Davies, D. R. and Burgess Hickman, A. 2006. Application of protein engineering to improve crystal properties. International Tables for Crystallography. F:4:4.3:100–110.

Author Information

  1. Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0560, USA

Publication History

  1. Published Online: 1 JAN 2006

Abstract

There is accelerating use of protein engineering by protein crystallographers. In this chapter, procedures that have been used successfully in protein crystallography are outlined. Topics covered include: improving solubility; use of fusion proteins; mutations to improve diffraction quality; avoiding protein heterogeneity; engineering crystal contacts to enhance crystallization in a particular crystal form; and engineering heavy-atom sites.

Keywords:

  • crystal quality;
  • crystallization;
  • fusion proteins;
  • heavy-atom sites in protein engineering;
  • mutations;
  • protein engineering;
  • protein heterogeneity;
  • improving solubility of proteins