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 Å. A 97.8% complete data set to 1.9 Å 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 Å. Data sets of wild-type crystals soaked with L-tryptophan or pyridoxal phosphate were collected, as well as of Y74F mutant soaked with both.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - 1 Nov 2004|
ASJC Scopus subject areas
- Structural Biology