title: Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae.
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.
authors.affiliation: Laboratory for Structural Biology, University of Alabama in Huntsville, MSB 203C, Huntsville, AL 35899, USA.
authors.forename: P H
authors.initials: PH
authors.lastname: Roberts
authors.forename: X
authors.initials: X
authors.lastname: Zhou
authors.forename: A M
authors.initials: AM
authors.lastname: Holmes
authors.forename: H
authors.initials: H
authors.lastname: Ranson
authors.forename: G
authors.initials: G
authors.lastname: Small
authors.forename: J
authors.initials: J
authors.lastname: Hemingway
authors.forename: J D
authors.initials: JD
authors.lastname: Ng
authors.forename: L
authors.initials: L
authors.lastname: Chen
authors.forename: E J
authors.initials: EJ
authors.lastname: Meehan
mesh_terms: D000818:Animals; D000852:Anopheles / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003634:DDT; D005982:Glutathione Transferase / Q000737:chemistry*; D007305:Insecticide Resistance; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D011994:Recombinant Proteins; D003634:DDT; D005982:Glutathione Transferase