Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium.
The tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium can be crystallized by the method of vapor diffusion from solutions of polyethylene glycol 8000 and various salts. Thin needles are obtained in the presence of a monovalent cation (Na+), thicker crystals are obtained in the presence of divalent cations (Mg2+, Mn2+, Fe2+, Ca2+, Zn2+), and square-faced crystals are obtained in the presence of spermine. Although the spermine and Mg2+ crystals differ in morphology, they are both monoclinic and in space group C2 with a = 184.5 A, b = 62.4 A, c = 67.7 A, beta = 94 degrees 40', and one alpha beta pair of Mr = 71,700/asymmetric unit. The crystals appear reasonably resistant to radiation damage and should be suitable for a complete structure investigation. The separated S. typhimurium alpha, holo-beta 2, and apo-beta 2 subunits do not crystallize under these conditions nor do the alpha 2 beta 2 complex or the alpha- or holo-beta 2 subunits from Escherichia coli or from an interspecies hybrid.
D002413:Cations, Divalent; D003460:Crystallization; D012486:Salmonella typhimurium / Q000201:enzymology*; D014367:Tryptophan Synthase; D014961:X-Ray Diffraction
D002413:Cations, Divalent; D014367:Tryptophan Synthase