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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 Å (pH 8.5) and a = 57.1, b = 77.0 and c = 81.5 Å (pH 4.6). Diffraction data to 1.82 Å for the pH 8.5 crystal and 2.33 Å for the pH 4.6 crystal were collected on a multiwire area detector using a rotating-anode X-ray generator.

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