Crystallization and preliminary crystallographic investigations of rhodanese from Azotobacter vinelandii

The rhdA gene identified in Azotobacter vinelandii codes for a protein, Rhd A, which displays rhodanese (thiosulfate-cyanide sulfurtransferase) activit y. RhdA was overexpressed and purified to homogeneity. The protein crystall ized in the orthorhombic space group P2(1)2(1)2 with unit-cell parameters a = 44.4, b = 150.8, c = 53.8 Angstrom: on a synchrotron source the diffract ion patterns could be collected to a resolution limit of 1.8 Angstrom. Eval uation of the crystal density indicates that the crystal lattice accommodat es one molecule per asymmetric unit and that the solvent content is 59% of the total volume.