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 P 3 1 21, with unit‐cell parameters a  =  b  = 116.83, c = 92.24 Å, and contain one protein molecule per asymmetric unit. The V M value and solvent content are 4.07 Å 3  Da −1 and 69.8%, respectively.