Purification and crystallization of a schistosomal glutathione S‐Transferase

Michele A. McTigue; Susan L. Bernstein; De Wight R. Williams; John A. Tainer

doi:10.1002/prot.340220108

Purification and crystallization of a schistosomal glutathione S‐Transferase

Michele A. McTigue, Susan L. Bernstein, De Wight R. Williams, John A. Tainer

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

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 Sj26^1,2 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 P6₃22 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.

Original language	English (US)
Pages (from-to)	55-57
Number of pages	3
Journal	Proteins: Structure, Function, and Bioinformatics
Volume	22
Issue number	1
DOIs	https://doi.org/10.1002/prot.340220108
State	Published - May 1995
Externally published	Yes

Keywords

X‐ray diffraction
crystailization
glutathione S‐transferase
helminth
schistosomiasis

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.340220108

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title = "Purification and crystallization of a schistosomal glutathione S‐Transferase",

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 Sj261,2 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 P6322 with unit cell dimensions a = b = 125.2 {\AA} and c = 72.0 {\AA} and contain one Sj26 monomer per asymmetric unit. A complete native diffraction data set has been obtained to 2.4 {\AA} resolution. {\textcopyright} 1995 Wiley‐Liss, Inc.",

keywords = "X‐ray diffraction, crystailization, glutathione S‐transferase, helminth, schistosomiasis",

author = "McTigue, {Michele A.} and Bernstein, {Susan L.} and Williams, {De Wight R.} and Tainer, {John A.}",

year = "1995",

month = may,

doi = "10.1002/prot.340220108",

language = "English (US)",

volume = "22",

pages = "55--57",

journal = "Proteins: Structure, Function, and Bioinformatics",

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publisher = "Wiley-Liss Inc.",

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T1 - Purification and crystallization of a schistosomal glutathione S‐Transferase

AU - McTigue, Michele A.

AU - Bernstein, Susan L.

AU - Williams, De Wight R.

AU - Tainer, John A.

PY - 1995/5

Y1 - 1995/5

N2 - 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 Sj261,2 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 P6322 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.

AB - 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 Sj261,2 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 P6322 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.

KW - X‐ray diffraction

KW - crystailization

KW - glutathione S‐transferase

KW - helminth

KW - schistosomiasis

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DO - 10.1002/prot.340220108

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JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

IS - 1

ER -

Purification and crystallization of a schistosomal glutathione S‐Transferase

Abstract

Keywords

ASJC Scopus subject areas

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