Crystallization and preliminary X-ray diffraction studies of the glutathione S-transferase from Plasmodium falciparum

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 Angstrom resolution were collected from an orthorhombic crystal form with unit-cell parameters a = 62.2, b = 88.3, c = 75.3 Angstrom. A search for heavy-atom derivatives has been initiated, along with phase-determination efforts by molecular replacement.