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Journal Article

Crystallization of membrane proteins


Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ostermeier, C., & Michel, H. (1997). Crystallization of membrane proteins. Current Opinion in Structural Biology, 7(5), 697-701. doi:10.1016/s0959-440x(97)80080-2.

Cite as: https://hdl.handle.net/21.11116/0000-0006-F25A-4
Five new membrane protein structures have been determined since 1995 using X-ray crystallography: bacterial light-harvesting complex; bacterial and mitochondrial cytochrome c oxidases; mitochondrial bc1 complex; and alpha-hemolysin. These successes are partly based on advances in the crystallization procedures for integral membrane proteins. Variation of the size of the detergent micelle and/or increasing the size of the polar surface of the membrane protein is the most important route to well-ordered membrane protein crystals. The use of bicontinuous lipidic cubic phases also appears to be promising.