| Literature DB >> 15652249 |
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.Mesh:
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Year: 2004 PMID: 15652249 PMCID: PMC2748814 DOI: 10.1016/j.pbiomolbio.2004.07.006
Source DB: PubMed Journal: Prog Biophys Mol Biol ISSN: 0079-6107 Impact factor: 3.667