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

Polyamine oxidase catalyses the oxidation of the secondary amino group of spermine, spermidine and their acetyl derivatives. The enzyme plays an important role in the regulation of polyamine intracellular concentration and is a member of the family of flavin-containing amine oxidases. Crystals of maize 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) with cell dimensions a = b = 184.6, c = 280.9 Angstrom. A native data set has been collected to 2.7 Angstrom resolution at a synchrotron radiation source.