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

Eun Hyuk Jang, Hyun Park, Ae Kyung Park, Jin Ho Moon, Young Min Chi, In Young Ahn

Research output: Contribution to journalArticle

3 Citations (Scopus)

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%.

Original languageEnglish
Pages (from-to)1132-1134
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number12
DOIs
Publication statusPublished - 2008 Nov 28

Keywords

  • CDNB
  • Glutathione
  • Glutathione S-transferases
  • ρ class

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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