PMID:22034843

Citation	Gabrielsen, M, Kroner, F, Black, I, Isaacs, NW, Roe, AJ and McLuskey, K High-throughput identification of purification conditions leads to preliminary crystallization conditions for three inner membrane proteins. Mol. Membr. Biol. 28:445-53
Abstract	An important factor in the crystallization, and subsequent structural determination, of integral membrane proteins is the ability to produce a stable and monodisperse solution of the protein. Obtaining the correct purification detergent to achieve this can be laborious and is often serendipitous. In this study, high-throughput methods are used to analyze the suitability of eight different detergents on the stability of 12 inner transmembrane proteins from Escherichia coli. The best results obtained from the small-scale experiments were scaled up, the aggregation state of the proteins assessed, and all monodisperse protein solutions entered into crystallization trials. This resulted in preliminary crystallization hits for three inner membrane proteins: XylH, PgpB and YjdL and this study reports the methods, purification procedures and crystallization conditions used to achieve this.
Links	PubMed Online version:10.3109/09687688.2011.628954
Keywords	Crystallization/methods; Detergents/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; High-Throughput Screening Assays; Membrane Proteins/chemistry; Membrane Proteins/isolation & purification; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/isolation & purification
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