Crystallization and preliminary X-ray diffraction studies of a glutathione S-Transferase from the Australian sheep blowfly, Lucilia cuprina

Matthew C.J. Wilce, Susanne C. Feil, Philip G. Board, Michael W. Parker

Research output: Contribution to journalArticleResearchpeer-review

10 Citations (Scopus)

Abstract

Crystals of a glutathione S-transferase from the Australian sheep blowfly Lucilia cuprina have been grown from ammonium sulphate by the hanging drop vapour diffusion method. Successful crystallization required the presence of the inhibitor S-hexylglutathione. The crystals belong to the tetragonal space group P41122 or P43322) with cell dimensions of a = b = 88·1 A ̊ and c = 66·9 A ̊. They contain one monomer in the asymmetric unit and diffract beyond 2·8 Å resolution.

Original languageEnglish
Pages (from-to)1407-1409
Number of pages3
JournalJournal of Molecular Biology
Volume236
Issue number5
DOIs
Publication statusPublished - 11 Mar 1994
Externally publishedYes

Keywords

  • crystals
  • detoxification
  • glutathione S-transferase
  • insecticides
  • X-ray crystallography

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