TY - JOUR
T1 - Membrane protein crystallization
T2 - observations and use of short chain phospholipids as amphiphiles
AU - Eiselé, Jean Luc
AU - Keller, Thomas A.
AU - König, Nicola
AU - Stauffer, Kathrin A.
AU - Rosenbusch, Jürg P.
AU - Low, Philip S.
PY - 1991/3/1
Y1 - 1991/3/1
N2 - An integral membrane protein, porin OmpF located in E. coli outer membrane, has been crystallized in the sole presence of short chain phospholipids. Although the amphiphilic characteristics of these molecules are comparable to those of conventional detergents, they appear to be unique probes for the study of the phospholipid-protein interactions by crystallographic methods. Here we also discuss the influence of the detergent head group on the crystal packing, and the role of additives. The stabilization of crystals after termination of growth in protein-free buffer is described.
AB - An integral membrane protein, porin OmpF located in E. coli outer membrane, has been crystallized in the sole presence of short chain phospholipids. Although the amphiphilic characteristics of these molecules are comparable to those of conventional detergents, they appear to be unique probes for the study of the phospholipid-protein interactions by crystallographic methods. Here we also discuss the influence of the detergent head group on the crystal packing, and the role of additives. The stabilization of crystals after termination of growth in protein-free buffer is described.
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U2 - 10.1016/0022-0248(91)90871-2
DO - 10.1016/0022-0248(91)90871-2
M3 - Article
AN - SCOPUS:0026119967
VL - 110
SP - 96
EP - 102
JO - Journal of Crystal Growth
JF - Journal of Crystal Growth
SN - 0022-0248
IS - 1-2
ER -