Pseudomonas aeruginosa L-arginine deiminase, an enzyme catalyzing the irreversible catabolism of arginine to citrulline, has been produced in selenomethionyl form. The protein was purified and crystallized by the sitting-drop vapour-diffusion method using a precipitant solution consisting of 55% MPD, 100 mM cacodylate pH 6.5, 20 mM MgCl2. Crystals display tetragonal symmetry (P41212 or P43212), with unit-cell parameters a = b = 106.0, c = 300.2 Å, and diffract to 2.7 Å. resolution. A complete MAD data set was collected to 3.2 Å resolution on beamline BM30 at ESRF.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 1 Dec 2002|