title: Practical considerations of membrane protein instability during purification and crystallisation.
abstract: Crystallisation of integral membranes requires milligrams of purified protein in a homogeneous, monodisperse state, and crucially, the membrane protein must also be fully functional and stable. The stability of membrane proteins in solution is dependent on the type of detergents used, but unfortunately the use of the most stabilising detergent can often decrease the probability of obtaining crystals that diffract to high resolution, especially of small membrane proteins. A number of strategies have been developed to facilitate the purification of membrane proteins in a functional form, which have led to new possibilities for structure determination.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, UK. cgt@mrc-lmb.cam.ac.uk
authors.forename: Christopher G
authors.initials: CG
authors.lastname: Tate
mesh_terms: D000818:Animals; D003460:Crystallization; D003902:Detergents / Q000737:chemistry; D005818:Genetic Engineering / Q000379:methods; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D008958:Models, Molecular; D011487:Protein Conformation; D055550:Protein Stability; D013696:Temperature
chemical_list: D003902:Detergents; D008565:Membrane Proteins