CRYSTALLIZATION AND X-RAY-DIFFRACTION STUDIES OF GLUTATHIONE-S-TRANSFERASE FROM ESCHERICHIA-COLI

Crystals of glutathione S-transferase from Escherichia coli have been obtained by use of polyethylene glycol 6000 as a precipitant. The crys tallization was performed in the presence of a glutathione sulfonate i nhibitor under the acidic condition, with combination of the sitting-d rop vapour-diffusion and the macro-seeding procedures. The crystals an of a thin-plate shape with typical sizes of 1.0 x 0.5 x 0.1 mm, and a re stable against X-ray irradiation. They belong to the space group P2 (1)2(1)2(1) with cell parameters of a = 90.47 Angstrom, b = 93.87 Angs trom and c = 51.10 Angstrom, and diffract X-rays at least up to 2.3 An gstrom resolution. The solvent content is 48% in volume, when a homodi meric molecule of the enzyme is assumed to occupy an asymmetric unit o f the crystal. The crystals are suitable for three-dimensional structu ral studies. Diffraction data of the native crystal have been collecte d.