一种血吸虫谷胱甘肽S-转移酶的纯化与结晶

Purification and crystallization of a schistosomal glutathione S-transferase.

作者信息

McTigue M A, Bernstein S L, Williams D R, Tainer J A

机构信息

Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA.

出版信息

Proteins. 1995 May;22(1):55-7. doi: 10.1002/prot.340220108.

DOI:10.1002/prot.340220108

PMID:7675787

Abstract

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 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 A and c = 72.0 A and contain one Sj26 monomer per asymmetric unit. A complete native diffraction data set has been obtained to 2.4 A resolution.

摘要

日本血吸虫26 kDa谷胱甘肽S-转移酶（Sj26）是一种潜在的抗血吸虫疫苗抗原，已以未结合配体的形式结晶。Sj26在大肠杆菌中重组表达，未使用谷胱甘肽亲和柱，以利于未结合酶的制备。重组蛋白包含Sj26的所有218个残基以及连接到C末端的另外13个残基。通过气相扩散法，以硫酸铵为沉淀剂，在pH 5.6条件下获得了重组Sj26晶体。这些晶体属于六方空间群P6(3)22，晶胞参数a = b = 125.2 Å，c = 72.0 Å，每个不对称单元包含一个Sj26单体。已获得分辨率为2.4 Å的完整天然衍射数据集。