Two-dimensional crystallization and electron crystallography of MAPEG proteins
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/209694
- author
- Hebert, Hans LU ; Jegerschold, C ; Bhakat, P and Holm, P J
- organization
- publishing date
- 2005
- 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
- 2016-04-01 15:46:55
- date last changed
- 2022-01-28 07:00:31
@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}},
doi = {{10.1016/S0076-6879(05)01010-4}},
volume = {{401}},
year = {{2005}},
}