Crystallization and preliminary X-ray studies of cold-active protein-tyrosine phosphatase of Shewanella sp.

Cold-active protein-tyrosine phosphatase (PTPase) of Shewanella sp. was expressed, purified and crystallized using the hanging-drop vapour-diffusion method at two different pH values (4.6 and 8.5). Both crystals are orthorhombic and belong to space group P212121, with unit-cell parameters a = 56.4, b = 76.8, c = 81.0 A (pH 8.5) and a = 57.1, b = 77.0 and c = 81.5 A (pH 4.6). Diffraction data to 1.82 A for the pH 8.5 crystal and 2.33 A for the pH 4.6 crystal were collected on a multiwire area detector using a rotating-anode X-ray generator.