Biology Reference
In-Depth Information
Summary
Crystallization of membrane proteins remains a major challenge in mod-
ern structural biology. The amphiphathic character of these proteins is
significant as well as the natural environment of these proteins being a
lipid bilayer. This chapter has described different techniques of mem-
brane protein crystallization focusing on a recent breakthrough: methods
of crystallization in the detergent-lipid environment ( in meso methods).
Major progress can be attributed to the application of the lipidic cubic
phase approach, but there is evidence that three other methods (sponge
phase, bicelles and vesicles) described in this chapter may also have a
more general application. Further development of in meso approaches is
needed in the future.
Acknowledgments
We are greatly indebted to A. Ishchenko, S. Golubev and O. Volkov for
providing valuable information on their unpublished experiments. We
would like to acknowledge Georg Bueld and Eva Pebay-Peyroula for con-
tinuous support of our work. Christian Baeken is gratefully acknowledged
for his help with protein production.
This chapter was updated based on our lecture notes for the 39th IFF
Spring School “Soft Matter — From Synthetic to Biological Materials,”
Forschungszentrum Jülich GmbH (www.fz-juelich.de/iff/fs2008_ prog_c).
References
Alfons K, Engstroem S. (1998) Drug compatibility with the sponge phases
formed in monoolein, water, and propylene glycol or poly (ethylene
glycol). J Pharm Sci 87 : 1527-1530.
Briggs J, Ching H, Caffrey M. (1996) The temperature-composition phase
diagram and mesophase structure characterization of the monoolein/
water system. J Phys II 6 : 723-751.
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