Crystallization and preliminary X-ray analysis of pollyamine oxidase from Zea mays L.

Polyamine oxidase catalyses the oxidation of the secondary amino group of s permine, spermidine and their acetyl derivatives. The enzyme plays an impor tant role in the regulation of polyamine intracellular concentration and is a member of the family of flavin-containing amine oxidases. Crystals of ma ize polyamine oxidase have been grown by the hanging-drop vapour-diffusion technique. The crystals are in hexagonal space group P6(1)22 (or P6(5)22) w ith cell dimensions a = b = 184.6, c = 280.9 Angstrom. A native data set ha s been collected to 2.7 Angstrom resolution at a synchrotron radiation sour ce.