Crystallization and preliminary crystallographic investigations of rhodanese from Azotobacter vinelandii
- 1 August 1999
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 55 (8) , 1471-1473
- https://doi.org/10.1107/s0907444999006526
Abstract
The rhdA gene identified in Azotobacter vinelandii codes for a protein, RhdA, which displays rhodanese (thiosulfate–cyanide sulfurtransferase) activity. RhdA was overexpressed and purified to homogeneity. The protein crystallized in the orthorhombic space group P21212 with unit-cell parameters a = 44.4, b = 150.8, c = 53.8 Å; on a synchrotron source the diffraction patterns could be collected to a resolution limit of 1.8 Å. Evaluation of the crystal density indicates that the crystal lattice accommodates one molecule per asymmetric unit and that the solvent content is 59% of the total volume.Keywords
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