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  • Title: Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.
    Author: Kogan A, Gdalevsky GY, Cohen-Luria R, Parola AH, Goldgur Y.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 Nov; 60(Pt 11):2073-5. PubMed ID: 15502331.
    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.
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