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Purification and crystallization of a schistosomal glutathione S-transferase.
Proteins. 1995 May; 22(1):55-7.P

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.

Authors+Show Affiliations

Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7675787

Citation

McTigue, M A., et al. "Purification and Crystallization of a Schistosomal Glutathione S-transferase." Proteins, vol. 22, no. 1, 1995, pp. 55-7.
McTigue MA, Bernstein SL, Williams DR, et al. Purification and crystallization of a schistosomal glutathione S-transferase. Proteins. 1995;22(1):55-7.
McTigue, M. A., Bernstein, S. L., Williams, D. R., & Tainer, J. A. (1995). Purification and crystallization of a schistosomal glutathione S-transferase. Proteins, 22(1), 55-7.
McTigue MA, et al. Purification and Crystallization of a Schistosomal Glutathione S-transferase. Proteins. 1995;22(1):55-7. PubMed PMID: 7675787.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and crystallization of a schistosomal glutathione S-transferase. AU - McTigue,M A, AU - Bernstein,S L, AU - Williams,D R, AU - Tainer,J A, PY - 1995/5/1/pubmed PY - 1995/5/1/medline PY - 1995/5/1/entrez SP - 55 EP - 7 JF - Proteins JO - Proteins VL - 22 IS - 1 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 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. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/7675787/Purification_and_crystallization_of_a_schistosomal_glutathione_S_transferase_ L2 - https://doi.org/10.1002/prot.340220108 DB - PRIME DP - Unbound Medicine ER -