PURIFICATION AND CRYSTALLIZATION OF A SCHISTOSOMAL GLUTATHIONE-S-TRANSFERASE

被引：13

作者：

MCTIGUE, MA ^{[1
]}

BERNSTEIN, SL ^{[1
]}

WILLIAMS, DR ^{[1
]}

TAINER, JA ^{[1
]}

机构：

[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1995年 / 22卷 / 01期

关键词：

SCHISTOSOMIASIS; HELMINTH; CRYSTALLIZATION; X-RAY DIFFRACTION; GLUTATHIONE S-TRANSFERASE;

D O I：

10.1002/prot.340220108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 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 obtained to 2.4 Angstrom resolution. (C) 1995 Wiley-Liss, Inc.

引用

页码：55 / 57

页数：3

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