PMID:15502331

Citation	Kogan, A, Gdalevsky, GY, Cohen-Luria, R, Parola, AH and Goldgur, Y (2004) Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase. Acta Crystallogr. D Biol. Crystallogr. 60:2073-5
Abstract	Tryptophanase from Escherichia coli is a pyridoxal phosphate-dependent homotetrametic enzyme with a subunit weight of 52 kDa. It has been crystallized in the apo form by the hanging-drop vapour-diffusion method using polyethylene glycol 400 as a precipitant and magnesium chloride as an additive. The crystals belong to the orthorhombic space group F222, with unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A. A 97.8% complete data set to 1.9 A resolution was collected at a rotating-anode source from a single frozen crystal. Packing-density considerations agree with a monomer in the asymmetric unit with a solvent content of 55%. Tryptophanase mutants W330F and Y74F were crystallized under the same conditions and the crystals diffracted to a resolution limit of 1.9 A. Data sets of wild-type crystals soaked with L-tryptophan or pyridoxal phosphate were collected, as well as of Y74F mutant soaked with both.
Links	PubMed Online version:10.1107/S0907444904022425
Keywords	Apoenzymes/chemistry; Apoenzymes/genetics; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Mutation/genetics; Tryptophan/genetics; Tryptophanase/chemistry; Tryptophanase/genetics; Tyrosine/genetics
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