title: Thermostable multicopper oxidase from Thermus thermophilus HB27: crystallization and preliminary X-ray diffraction analysis of apo and holo forms.
abstract: A thermostable multicopper oxidase from Thermus thermophilus HB27 (Tth-MCO) was successfully crystallized using the sitting-drop and hanging-drop vapour-diffusion methods. Crystallization conditions and preliminary X-ray diffraction data to 1.5 Å resolution obtained using synchrotron radiation at 100 K are reported. The crystals belonged to space group C222(1), with unit-cell parameters a = 93.6, b = 110.3, c = 96.3 Å. A monomer in the asymmetric unit yielded a Matthews coefficient (V(M)) of 2.60 Å(3) Da(-1) and a solvent content of 53%. An inactive enzyme form, apo-Tth-MCO, was also crystallized and diffraction data were collected to 1.7 Å resolution. In addition, a second inactive form of the enzyme, Hg-Tth-MCO, was obtained by soaking apo-Tth-MCO crystals with mercury(II) chloride and data were collected to a resolution of 1.7 Å.
authors.affiliation: Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, UNAM, Chamilpa, Cuernavaca, Morelos, Mexico. serrano@ibt.unam.mx
authors.forename: Hugo
authors.initials: H
authors.lastname: Serrano-Posada
authors.forename: Brenda
authors.initials: B
authors.lastname: Valderrama
authors.forename: Vivian
authors.initials: V
authors.lastname: Stojanoff
authors.forename: Enrique
authors.initials: E
authors.lastname: Rudiño-Piñera
mesh_terms: D001051:Apoenzymes / Q000737:chemistry; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D020035:Holoenzymes / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry*; D016963:Thermus thermophilus / Q000201:enzymology*
chemical_list: D001051:Apoenzymes; D020035:Holoenzymes; D010088:Oxidoreductases; C024748:copper oxidase