The complex of Tamarindus indica Kunitz-type trypsin inhibitor and porcine trypsin has been crystallized by the sitting-drop vapour-diffusion method using ammonium acetate as precipitant and sodium acetate as buffer. The homogeneity of complex formation was checked by size-exclusion chromatography and further confirmed by reducing SDS-PAGE. The crystals diffracted to 2.0 angstrom resolution and belonged to the tetragonal space group P4(1), with unit-cell parameters a = b = 57.1, c = 120.1 angstrom. Preliminary X-ray diffraction analysis indicated the presence of one unit of inhibitor-trypsin complex per asymmetric unit, with a solvent content of 45%.
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| http://dx.doi.org/10.1107/S1744309109041694 | DOI Listing |
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