Abstract
A major advance in the study of integral membrane protein structure has been the development of methods for crystallizing these amphiphilic protein species. The crystals were obtained from isotropic solutions of protein and nonionic detergents and contain a substantial amount of detergent bound within the crystal lattice. Standard techniques for crystallizing water-soluble proteins can be applied to membrane proteins if the physical characteristics and behavior of the detergent system used for protein solubilization are adequately controlled. In this report we present the results of some crystallization experiments on porin, a protein forming transmembrane channels in the outer membrane of E. coli, and discuss the detergent-related phenomena which seem to affect the crystallization process.
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