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

Crystallization and preliminary X‐ray crystallographic studies of the ρ‐class glutathione S... 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 ρ‐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 Å 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%. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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References (13)

Publisher
Wiley
Copyright
International Union of Crystallography, 2008
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309108034003
pmid
19052367
Publisher site
See Article on Publisher Site

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 ρ‐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 Å 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%.

Journal

Acta Crystallographica Section FWiley

Published: Dec 1, 2008

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