title: Crystallization and a preliminary X-ray diffraction study of isozyme 3-3 of glutathione S-transferase from rat liver.
abstract: Crystals of the homodimeric isozyme 3-3 of glutathione S-transferase from rat liver have been obtained with the hanging drop method of vapor diffusion from ammonium sulfate solutions. The successful crystallization of the enzyme required the presence of both the enzyme inhibitor (9R, 10R)-9, 10-dihydro-9-(S-glutathionyl)-10-hydroxyphenanthrene and the detergent beta-octylglucopyranoside. The crystals belong to the monoclinic space group C2, with cell dimensions of a = 88.24(8) A, b = 69.44(4) A, c = 81.28(5) A, beta = 106.01(6) degrees, and contain four dimeric enzyme molecules per unit cell. The crystals diffract to at least 2.2 A and are suitable for X-ray crystallographic structure determination at high resolution.
authors: Department of Chemistry and Biochemistry, University of Maryland College Park 20742.
authors: M A
authors: MA
authors: Sesay
authors: H L
authors: HL
authors: Ammon
authors: R N
authors: RN
authors: Armstrong
mesh_terms: D000818:Animals; D003460:Crystallization; D005982:Glutathione Transferase; D007527:Isoenzymes; D008099:Liver / Q000201:enzymology*; D051381:Rats; D014961:X-Ray Diffraction
chemical_list: D007527:Isoenzymes; D005982:Glutathione Transferase