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

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)96-102
Number of pages7
JournalJournal of Crystal Growth
Volume110
Issue number1-2
DOIs
StatePublished - Mar 1 1991

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Inorganic Chemistry
  • Materials Chemistry

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