Literature DB >> 2769766

Crystallization of GST2, a human class alpha glutathione transferase.

S W Cowan1, T Bergfors, T A Jones, G Tibbelin, B Olin, P G Board, B Mannervik.   

Abstract

Single crystals of human GST2, a class alpha glutathione transferase have been grown in polyethylene glycol 2000 by the hanging-drop vapour diffusion method. The crystals belong to space group C2 and have cell dimensions a = 100.8 A, b = 95.4 A, c = 105.2 A and beta = 92.4 degrees. The X-ray diffraction pattern extends to better than 3 A resolution.

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Year:  1989        PMID： 2769766     DOI： 10.1016/0022-2836(89)90398-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  4 in total

1.  The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase.

Authors:  P G Board; B Mannervik
Journal:  Biochem J       Date:  1991-04-01       Impact factor: 3.857

2.  Effects of directed mutagenesis on conserved arginine residues in a human Class Alpha glutathione transferase.

Authors:  G Stenberg; P G Board; I Carlberg; B Mannervik
Journal:  Biochem J       Date:  1991-03-01       Impact factor: 3.857

3.  Site-directed mutagenesis and chemical modification of cysteine residues of rat glutathione S-transferase 3-3.

Authors:  W L Chen; J C Hsieh; J L Hong; S P Tsai; M F Tam
Journal:  Biochem J       Date:  1992-08-15       Impact factor: 3.857

4.  The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 A resolution.

Authors:  P Reinemer; H W Dirr; R Ladenstein; J Schäffer; O Gallay; R Huber
Journal:  EMBO J       Date:  1991-08       Impact factor: 11.598
  4 in total

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