title: Purification, crystallization and preliminary X-ray diffraction analysis of royal palm tree (Roystonea regia) peroxidase.
abstract: 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 A. The crystals belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 116.83, c = 92.24 A, and contain one protein molecule per asymmetric unit. The V(M) value and solvent content are 4.07 A3 Da(-1) and 69.8%, respectively.
authors.affiliation: Instituto de Física de São Carlos, Departamento de Física e Informática, Universidade de São Paulo, Avenida Trabalhador São Carlense 400, CEP 13566-590 São Carlos, SP, Brazil.
authors.forename: Leandra
authors.initials: L
authors.lastname: Watanabe
authors.forename: Alessandro S
authors.initials: AS
authors.lastname: Nascimento
authors.forename: Laura S
authors.initials: LS
authors.lastname: Zamorano
authors.forename: Valery L
authors.initials: VL
authors.lastname: Shnyrov
authors.forename: Igor
authors.initials: I
authors.lastname: Polikarpov
mesh_terms: D028023:Arecaceae / Q000201:enzymology*; D003460:Crystallization; D008970:Molecular Weight; D010544:Peroxidases / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014197:Trees / Q000201:enzymology; D014961:X-Ray Diffraction
chemical_list: D010940:Plant Proteins; D010544:Peroxidases