International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by E. Arnold, D. M. Himmel and M. G. Rossmann

International Tables for Crystallography (2012). Vol. F, ch. 3.2, p. 96

Section 3.2.5. Summary

J. A. Ernst,a,b D. G. Yansurac and C. M. Kothd*

aDepartment of Protein Chemistry, Genentech, 1 DNA Way, South San Francisco, California 94080, USA,bDepartment of Protein Engineering, Genentech, 1 DNA Way, South San Francisco, California 94080, USA,cDepartment of Antibody Engineering, Genentech, 1 DNA Way, South San Francisco, California 94080, USA, and dDepartment of Structural Biology, Genentech, 1 DNA Way, South San Francisco, California 94080, USA
Correspondence e-mail:  koth.christopher@gene.com

3.2.5. Summary

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There are many possible routes for the expression and isolation of membrane proteins for structural studies, and many factors can affect the likelihood of obtaining diffraction-quality crystals. The daunting prospect for almost any new membrane target is that every stage, including expression, solubilization, purification and crystallization, will prove challenging. In this light, it is encouraging that remarkably similar techniques have been employed for many successfully crystallized membrane targets, including, for example, the observation that most structures have been solved using just a handful of different detergents throughout the isolation and crystallization steps. It is equally significant that simple two-step purification strategies predominate. Clearly, new methods for the production of membrane proteins will continue to be developed. Nevertheless, for a field that is quite likely to be entering an acute phase of growth, a solid foundation has been established for reasonable `first-try' strategies.








































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