title: Crystallization of membrane proteins.
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.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. osti@laplace.csb.yale.edu
authors.forename: C
authors.initials: C
authors.lastname: Ostermeier
authors.forename: H
authors.initials: H
authors.lastname: Michel
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D003902:Detergents / Q000378:metabolism; D008055:Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D003902:Detergents; D008055:Lipids; D008565:Membrane Proteins