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

Citation
Ph. Roberts et al., Crystallization of agGST1-6, a recombinant glutathione S-transferase from a DDT-resistant strain of Anopheles gambiae, ACT CRYST D, 57, 2001, pp. 134-136
Citations number
16
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
0907-4449 → ACNP
Volume
57
Year of publication
2001
Part
1
Pages
134 - 136
Database
ISI
SICI code
0907-4449(200101)57:<134:COAARG>2.0.ZU;2-E
Abstract
Glutathione S-transferases (GSTs) belong to a family of detoxification enzy mes that conjugate glutathione to various xenobiotics, thus facilitating th eir expulsion from the cell. GST activity is elevated in many insecticide-r esistant insects, including the DDT-resistant malaria vector Anopheles gamb iae. Crystals of the recombinant form of a GST from A. gambiae, agGST1-6, h ave been grown in at least five different crystal forms, with a broad range of diffraction resolution limits. A complete 2.0 Angstrom data set has bee n collected on a C-centered orthorhombic crystal form with unit-cell parame ters a = 99.0, b = 199.4, c = 89.6 Angstrom. A search for heavy-atom deriva tives has been initiated, along with phase-determination efforts by molecul ar replacement.