Two-dimensional crystallization and electron crystallography of MAPEG proteins

Hans Hebert, C Jegerschold, P Bhakat, P J Holm

Research output: Contribution to journalReview articlepeer-review

4 Citations (SciVal)

Abstract

Members of the membrane-associated proteins in the eicosanoid and glutathione metabolism (MAPEG) superfamily have been subjected to two-dimensional crystallization experiments. A common denominator for successful attempts has been the use of a low lipid/protein ratio in the range of 1-9 (mol/mol). Electron crystallography demonstrated either hexagonal or orthorhombic packing of trimeric protein units. Three-dimensional structure analysis of the MAPEG member microsomal glutathione transferase 1 has shown that the monomer for this protein contains a left-handed bundle of four transmembrane helices. It is likely that this is a common structural motif for MAPEG proteins, because projection maps of all structurally characterized members are very similar.
Original languageEnglish
Pages (from-to)161
JournalMethods in Enzymology
Volume401
DOIs
Publication statusPublished - 2005

Subject classification (UKÄ)

  • Biological Sciences

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