Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae

Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):134-6. doi: 10.1107/s0907444900013810.

Abstract

Glutathione S-transferases (GSTs) belong to a family of detoxification enzymes that conjugate glutathione to various xenobiotics, thus facilitating their expulsion from the cell. GST activity is elevated in many insecticide-resistant insects, including the DDT-resistant malaria vector Anopheles gambiae. Crystals of the recombinant form of a GST from A. gambiae, agGST1-6, have been grown in at least five different crystal forms, with a broad range of diffraction resolution limits. A complete 2.0 A data set has been collected on a C-centered orthorhombic crystal form with unit-cell parameters a = 99.0, b = 199.4, c = 89.6 A. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anopheles / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • DDT*
  • Glutathione Transferase / chemistry*
  • Insecticide Resistance*
  • Protein Conformation
  • Recombinant Proteins / chemistry

Substances

  • Recombinant Proteins
  • DDT
  • Glutathione Transferase