title: Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes.
abstract: FAD synthetase from Corynebacterium ammoniagenes (CaFADS), a prokaryotic bifunctional enzyme that catalyses the phosphorylation of riboflavin as well as the adenylylation of FMN, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Diffraction-quality cubic crystals of native and selenomethionine-labelled (SeMet-CaFADS) protein belonged to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 133.47 A and a = b = c = 133.40 A, respectively. Data sets for native and SeMet-containing crystals were collected to 1.95 and 2.42 A resolution, respectively.
authors.affiliation: Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Institute of Biocomputation and Physics of Complex Systems, Universidad de Zaragoza, 50009 Zaragoza, Spain.
authors.forename: Beatriz
authors.initials: B
authors.lastname: Herguedas
authors.forename: Marta
authors.initials: M
authors.lastname: Martínez-Júlvez
authors.forename: Susana
authors.initials: S
authors.lastname: Frago
authors.forename: Milagros
authors.initials: M
authors.lastname: Medina
authors.forename: Juan A
authors.initials: JA
authors.lastname: Hermoso
mesh_terms: D003352:Corynebacterium / Q000201:enzymology* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012645:Selenomethionine / Q000737:chemistry
chemical_list: D011994:Recombinant Proteins; D012645:Selenomethionine; D009713:Nucleotidyltransferases; C020143:FMN adenylyltransferase