title: Crystallization of the extracellular rubber oxygenase RoxA from Xanthomonas sp. strain 35Y.
abstract: Rubber oxygenase A (RoxA) from Xanthomonas sp. strain 35Y is an extracellular dioxygenase that is capable of cleaving the double bonds of poly(cis-1,4-isoprene) into short-chain isoprene units with 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al (ODTD) as the major cleavage product. Crystals of the dihaem c-type cytochrome RoxA were grown by sitting-drop vapour diffusion using polyethylene glycol as a precipitant. RoxA crystallized in space group P2(1), with unit-cell parameters a = 72.4, b = 97.1, c = 101.1 A, beta = 98.39 degrees, resulting in two monomers per asymmetric unit. Diffraction data were collected to a limiting resolution of 1.8 A. Despite a protein weight of 74.1 kDa and only two iron sites per monomer, phasing was successfully carried out by multiple-wavelength anomalous dispersion.
authors.affiliation: Abteilung Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
authors.forename: Maren
authors.initials: M
authors.lastname: Hoffmann
authors.forename: Reinhard
authors.initials: R
authors.lastname: Braaz
authors.forename: Dieter
authors.initials: D
authors.lastname: Jendrossek
authors.forename: Oliver
authors.initials: O
authors.lastname: Einsle
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D010105:Oxygenases / Q000737:chemistry*; D011487:Protein Conformation; D014974:Xanthomonas / Q000201:enzymology*
chemical_list: D010105:Oxygenases