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Crystals of the catalytic core domain of a Trichoderma reesei β-­mannanase belonging to glycoside hydrolase family 5 have been grown by the sitting-drop method at room temperature using ammonium sulfate as precipitant. The crystals grow as thin colourless plates and belong to space group P21, with unit-cell parameters a = 50.0, b = 54.3, c = 60.2 Å, β = 111.3°, and have a single monomer of mannanase in the asymmetric unit. Native data to 2.0 Å resolution have been collected at room temperature using synchrotron radiation. Data for a platinum derivative have been collected to 1.65 Å at 110 K in a very short time at the CCLRC Daresbury synchrotron source, using a charge-coupled device (CCD) as detector.
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