title: Crystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium.
abstract: Tyrosinases are type 3 copper enzymes that are involved in the production of melanin and have two copper ions in the active site. Here, the crystallization and primary analysis of a tyrosinase from Bacillus megaterium is reported. The purified protein was crystallized in the absence or presence of zinc ions and the crystals diffracted to a resolution of 2.0 A. Crystals obtained in the presence of zinc belonged to space group P2(1)2(1)2(1), while crystals grown in the absence of zinc belonged to space group P2(1). In both space groups the asymmetric unit contained a dimer, with minor differences in the crystal density and in packing interactions.
authors.affiliation: Department of Biotechnology and Food Engineering, Technion-Israel Institute of Technology, Haifa 32000, Israel.
authors.forename: Mor
authors.initials: M
authors.lastname: Sendovski
authors.forename: Margarita
authors.initials: M
authors.lastname: Kanteev
authors.forename: Vered
authors.initials: V
authors.lastname: Shuster Ben-Yosef
authors.forename: Noam
authors.initials: N
authors.lastname: Adir
authors.forename: Ayelet
authors.initials: A
authors.lastname: Fishman
mesh_terms: D001410:Bacillus megaterium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D014442:Monophenol Monooxygenase / Q000737:chemistry*; D017434:Protein Structure, Tertiary
chemical_list: D014442:Monophenol Monooxygenase
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