Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp strain ADP

The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 angstrom resolution and adopted space group P2(1), with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 angstrom, beta = 106.6 degrees.