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.
N1 - Funding Information:
We thank Dr. R.M. Garavlto for his valuable advice and suggestionsa t the beginning of tins work, Drs. J.A. Jenkins, Z. Markovic-Housley, R.A. Pauptlt and J.N. Jansonlus for helpful discussions,a nd Dr. G.A. Bentley for careful reading of tins manuscript.T his work has been supported by Swiss National Science Foundauon grant 3.294.85,b y Roche Research Foundation and by Sandoz Forschung und Entwxcklung. J.-U Eisel6 is supported by EMBO Long-Term Fellowsinp ALTF 171-1988 and wishes to thank Dr R,J. Poljak for has contmuouss upport and interest.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
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 -