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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 57; no. 1; pp. 134 - 136
• Main Authors: Roberts, Pamela H., Zhou, Xiaoyin, Holmes, Anna M., Ranson, Hilary, Small, Graham, Hemingway, Janet, Ng, Joseph D., Chen, Liqing, Meehan, Edward J.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.01.2001
• Subjects: Animals; Anopheles - enzymology; Crystallization; Crystallography, X-Ray; DDT; Glutathione Transferase - chemistry; glutathione-S-transferases; Insecticide Resistance; malaria; Protein Conformation; Recombinant Proteins - chemistry
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444900013810

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 Å 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 Å. A search for heavy‐atom derivatives has been initiated, along with phase‐determination efforts by molecular replacement.