Membrane protein crystallization: observations and use of short chain phospholipids as amphiphiles

Jean Luc Eiselé; Thomas A. Keller; Nicola König; Kathrin A. Stauffer; Jürg P. Rosenbusch; Philip S. Low

doi:10.1016/0022-0248(91)90871-2

Membrane protein crystallization: observations and use of short chain phospholipids as amphiphiles

Jean Luc Eiselé, Thomas A. Keller, Nicola König, Kathrin A. Stauffer, Jürg P. Rosenbusch, Philip S. Low

Houston Methodist

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	96-102
Number of pages	7
Journal	Journal of Crystal Growth
Volume	110
Issue number	1-2
DOIs	https://doi.org/10.1016/0022-0248(91)90871-2
State	Published - Mar 1 1991

ASJC Scopus subject areas

Condensed Matter Physics
Inorganic Chemistry
Materials Chemistry

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10.1016/0022-0248(91)90871-2

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title = "Membrane protein crystallization: observations and use of short chain phospholipids as amphiphiles",

abstract = "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.",

author = "Eisel{\'e}, \{Jean Luc\} and Keller, \{Thomas A.\} and Nicola K{\"o}nig and Stauffer, \{Kathrin A.\} and Rosenbusch, \{J{\"u}rg P.\} and Low, \{Philip S.\}",

note = "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.",

year = "1991",

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doi = "10.1016/0022-0248(91)90871-2",

language = "English (US)",

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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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EP - 102

JO - Journal of Crystal Growth

JF - Journal of Crystal Growth

IS - 1-2

ER -

Membrane protein crystallization: observations and use of short chain phospholipids as amphiphiles

Abstract

ASJC Scopus subject areas

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