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Two-dimensional crystallization and electron crystallography of MAPEG proteins

Hebert, Hans LU ; Jegerschold, C; Bhakat, P and Holm, P J (2005) In Methods in Enzymology 401. p.161-161
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Methods in Enzymology
volume
401
pages
161 - 161
publisher
Academic Press
external identifiers
  • wos:000234746200010
  • pmid:16399385
  • scopus:30144433309
ISSN
0076-6879
DOI
10.1016/S0076-6879(05)01010-4
language
English
LU publication?
yes
id
8505730a-52d0-42f9-a978-bf484bffd125 (old id 209694)
date added to LUP
2007-09-28 08:46:03
date last changed
2017-01-01 06:46:30
@article{8505730a-52d0-42f9-a978-bf484bffd125,
  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.},
  author       = {Hebert, Hans and Jegerschold, C and Bhakat, P and Holm, P J},
  issn         = {0076-6879},
  language     = {eng},
  pages        = {161--161},
  publisher    = {Academic Press},
  series       = {Methods in Enzymology},
  title        = {Two-dimensional crystallization and electron crystallography of MAPEG proteins},
  url          = {http://dx.doi.org/10.1016/S0076-6879(05)01010-4},
  volume       = {401},
  year         = {2005},
}