PURIFICATION AND CRYSTALLIZATION OF A SCHISTOSOMAL GLUTATHIONE-S-TRANSFERASE

The 26-kDa glutathione S-transferase from Schistosoma japonica (Sj26), a potential antischistosomal vaccine antigen, has been crystallized i n an unligated form. Sj26 was recombinantly produced in E. coli withou t using a glutathione affinity column to facilitate preparation of unl igated enzyme. The recombinant protein contains all 218 residues of Sj 26(1,2) and an additional 13 residues linked to the C-terminus. Crysta ls of recombinant Sj26 were obtained by the vapor diffusion method usi ng ammonium sulfate as the precipitant at pH 5.6. The crystals belong to the hexagonal space group P6(3)22 with unit cell dimensions a = b = 125.2 Angstrom and c = 72.0 Angstrom and contain one Sj26 monomer per asymmetric unit. A complete native diffraction data set has been obta ined to 2.4 Angstrom resolution. (C) 1995 Wiley-Liss, Inc.