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Crystallization and preliminary X-ray crystallographic studies of the rho-class glutathione S-transferase from the Antarctic clam Laternula elliptica

Cited 2 time in scopus
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Title
Crystallization and preliminary X-ray crystallographic studies of the rho-class glutathione S-transferase from the Antarctic clam Laternula elliptica
Other Titles
남극큰띠조개 유래의 rho-class glutathione S-transferase의 X-ray crystallographic 연구
Authors
Ahn, In-Young
Park, Ae-Kyung
Park, Hyun
Jang, Eun Hyuk
Chi, Young Min
Moon, Jin Ho
Subject
Biochemistry & Molecular Biology; Biophysics; Crystallography
Keywords
Antarctic clam; Glutathione S-transferases; Laternula elliptica; X-ray crystallography; structure
Issue Date
2008
Publisher
BLACKWELL PUBLISHING
Citation
Ahn, In-Young, et al. 2008. "Crystallization and preliminary X-ray crystallographic studies of the rho-class glutathione S-transferase from the Antarctic clam Laternula elliptica". ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 64(1): 1132-1134.
Abstract
Glutathione S-transferases are involved in phase II detoxification processes and catalyze the nucleophilic attack of the tripeptide glutathione on a wide range of endobiotic and xenobiotic electrophilic substrates. The _-class glutathione S-transferase from Laternula elliptica was overexpressed in Escherichia coli, purified and crystallized with two substrates: glutathione and 1-chloro-2,4-dinitrobenzene (CDNB). Diffraction data were collected to 2.20 Å resolution for the glutathione-complex crystals and to 2.00 A ˚ resolution for the CDNB complex crystals using a synchrotron-radiation source. Both crystals belonged to the C-centred monoclinic space group C2. The unit-cell parameters for the CDNB-complex crystals were a = 89.66, b = 59.27, c = 55.45 Å, β = 124.52°. The asymmetric unit contained one molecule, with a corresponding VM of 2.36 Å3 Da-1 and a solvent content of 47.8%.
URI
http://repository.kopri.re.kr/handle/201206/6391
DOI
http://dx.doi.org/10.1107/S1744309108034003
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