title: Crystallization and preliminary X-ray diffraction studies of the glutathione S-transferase from Plasmodium falciparum.
abstract: Glutathione S-transferases (GSTs) belong to a family of detoxification enzymes that conjugate glutathione to various xenobiotics, thus facilitating their expulsion from the cells. For high-resolution crystallographic investigations, GST from the human malarial parasite Plasmodium falciparum was overexpressed in bacterial cells and crystallized using hanging-drop vapour diffusion. X-ray intensity data to 2.8 A resolution were collected from an orthorhombic crystal form with unit-cell parameters a = 62.2, b = 88.3, c = 75.3 A. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.
authors.affiliation: Department of Biochemistry, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Strasse 74, 20359 Hamburg, Germany.
authors.forename: C
authors.initials: C
authors.lastname: Burmeister
authors.forename: M
authors.initials: M
authors.lastname: Perbandt
authors.forename: Ch
authors.initials: Ch
authors.lastname: Betzel
authors.forename: R D
authors.initials: RD
authors.lastname: Walter
authors.forename: E
authors.initials: E
authors.lastname: Liebau
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D005982:Glutathione Transferase / Q000737:chemistry*; D010963:Plasmodium falciparum / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D013696:Temperature; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D005982:Glutathione Transferase