Crystallization of membrane proteins
Current Opinion in Structural BiologyPublished 1 October 1997Open access
Christian Ostermeier, Hartmut Michel
Citations440
SJR quartileQ1
SJR score2.91
SNIP1.48
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TL;DR
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.
Abstract
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.
Keywords
Biochemistry, Genetics and Molecular Biology
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