International Tables for Crystallography

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International Tables for Crystallography (2006). Vol. F, ch4.3
Application of protein engineering to enhance crystallizability and improve crystal properties
Z. S. Derewenda. International Tables for Crystallography (2012). Vol. F, ch. 4.3, pp. 129-139  [ doi:10.1107/97809553602060000814 ]

Abstract

Until recently, protein crystallization has mostly been regarded as a stochastic event over which the investigator has little or no control. With the dramatic technological advances in synchrotron-radiation sources and detectors and the equally impressive progress in crystallographic software, including automated model building and validation, crystallization has increasingly become the rate-limiting step in X-ray diffraction studies of macromolecules. However, with the advent of recombinant methods it has also become possible to engineer target proteins and their complexes for higher propensity to form crystals with desirable X-ray diffraction qualities. As most proteins that are under investigation today are obtained by heterologous overexpression, these tech­niques hold the promise of becoming routine tools with the potential to transform classical crystallization screening into a more rational high-success-rate approach. This chapter presents an overview of protein-engineering methods designed to enhance crystallizability and discusses a number of examples of their successful application.


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About International Tables for Crystallography

International Tables for Crystallography is the definitive resource and reference work for crystallography. The multi-volume series comprises articles and tables of data relevant to crystallographic research and to applications of crystallographic methods in all sciences concerned with the structure and properties of materials.