title: Crystallization and preliminary X-ray analysis of cholesterol oxidase from Brevibacterium sterolicum containing covalently bound FAD.
abstract: Single crystals of cholesterol oxidase from Brevibacterium sterolicum containing a covalently bound form of the FAD cofactor have been obtained. The crystals are grown by vapor diffusion using the hanging drop technique from 12% polyethylene glycol, Mr 8000, and 75 mM MnSO4 as the precipitant at pH 5.2. In order to obtain large diffraction quality crystals, nucleation must occur at 22 degrees C with subsequent growth at 17 degrees C. The crystals belong to the monoclinic space group P21 with cell dimensions a = 78. 5 A, b = 126.7 A, c = 82.4 A and beta = 108.9 degrees with two protein molecules per asymmetric unit. Diffraction of these crystals has been observed to at least 2.2 A resolution and they are suitable for an X-ray structure analysis.
authors.affiliation: Biochemistry Department, Montreal Joint Centre for Structural Biology, McIntyre Medical Sciences Building, McGill University, 3655 Drummond Street, Montréal, Québec, H3G 1Y6, Canada.
authors.forename: N
authors.initials: N
authors.lastname: Croteau
authors.forename: A
authors.initials: A
authors.lastname: Vrielink
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D001951:Brevibacterium / Q000201:enzymology*; D002789:Cholesterol Oxidase / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry* / Q000302:isolation & purification; D011485:Protein Binding; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D005182:Flavin-Adenine Dinucleotide; D002789:Cholesterol Oxidase