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Purification and crystallization of a schistosomal glutathione S ‐Transferase
Author(s) -
McTigue Michele A.,
Bernstein Susan L.,
Williams DeWight R.,
Tainer John A.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220108
Subject(s) - ammonium sulfate , recombinant dna , crystallization , monomer , chemistry , resolution (logic) , transferase , glutathione , glutathione s transferase , antigen , glutathione transferase , enzyme , biochemistry , crystallography , chromatography , biology , gene , organic chemistry , immunology , polymer , artificial intelligence , computer science
The 26‐kDa glutathione S ‐transferase from Schistosoma japonica (Sj26), a potential antischistosomal vaccine antigen, has been crystallized in an unligated form. Sj26 was recombinantly produced in E. coli without using a glutathione affinity column to facilitate preparation of unligated enzyme. The recombinant protein contains all 218 residues of Sj26 1,2 and an additional 13 residues linked to the C‐terminus. Crystals of recombinant Sj26 were obtained by the vapor diffusion method using ammonium sulfate as the precipitant at pH 5.6. The crystals belong to the hexagonal space group P 6 3 22 with unit cell dimensions a = b = 125.2 Å and c = 72.0 Å and contain one Sj26 monomer per asymmetric unit. A complete native diffraction data set has been obtained to 2.4 Å resolution. © 1995 Wiley‐Liss, Inc.