title: Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath).
abstract: Methane monooxygenase is a multicomponent enzyme system that catalyzes the conversion of methane to methanol in methanotrophic bacteria. Catalysis occurs at non-heme dinuclear iron centers contained in the hydroxylase component of the system, a dimer of composition alpha 2 beta 2 gamma 2. The hydroxylase protein from Methylococcus capsulatus (Bath) has been crystallized from aqueous solutions containing polyethylene glycol, lithium sulfate, and ammonium acetate. The crystals are orthorhombic, space group P2(1)2(1)2(1), with one dimer of relative molecular mass M(r) = 252,000 in the asymmetric unit. The unit cell dimensions are a = 62.6 A, b = 110.1 A, c = 333.5 A. The crystals diffract uniformly beyond 2.5 A resolution. Crystals of the related hydroxylase from Methylosinus trichosporium OB3b have also been obtained.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
authors.forename: A C
authors.initials: AC
authors.lastname: Rosenzweig
authors.forename: C A
authors.initials: CA
authors.lastname: Frederick
authors.forename: S J
authors.initials: SJ
authors.lastname: Lippard
mesh_terms: D003460:Crystallization; D008772:Methylococcaceae / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D010105:Oxygenases / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D006899:Mixed Function Oxygenases; D010105:Oxygenases; C021555:methane monooxygenase