Purification, crystallization and preliminary X-ray diffraction analysis of royal palm tree ( Roystonea regia) peroxidase.

Royal palm tree peroxidase (RPTP), which was isolated from Roystonea regia leaves, has an unusually high stability that makes it a promising candidate for diverse applications in industry and analytical chemistry [Caramyshev et al. (2005), Biomacromolecules, 6, 1360–1366]. Here, the purification and crystallization of this plant peroxidase and its X-ray diffraction data collection are described. RPTP crystals were obtained by the hanging-drop vapour-diffusion method and diffraction data were collected to a resolution of 2.8 Å. The crystals belong to the trigonal space group P3121, with unit-cell parameters a =  b = 116.83, c = 92.24 Å, and contain one protein molecule per asymmetric unit. The VM value and solvent content are 4.07 Å3 Da−1 and 69.8%, respectively. [ABSTRACT FROM AUTHOR]