Membrane protein crystallization in amphiphile phases: practical and theoretical considerations
Authors:
Nollert Peter
Affiliation:
deCODE BioStructures, 7869 NE Day Rd. W, Bainbridge Island, WA 98110, USA
Abstract:
Integral membrane proteins are amphiphilic molecules. In order to enable chromatographic purification and crystallization, a complementary amphiphilic microenvironment must be created and maintained. Various types of amphiphilic phases have been employed in crystallizations and intricate amphiphilic microenvironmental structures have resulted from these and are found inside membrane protein crystals. In this review the process of crystallization is put into the context of amphiphile phase transitions. Finally, practical factors are considered and a pragmatic way is suggested to pursue membrane protein crystallization trials.