title: Crystallization and preliminary X-ray diffraction studies of nucleoside diphosphate kinase from Dictyostelium discoideum.
abstract: Nucleoside diphosphate kinase from the slime mold Dictyostelium discoideum is highly homologous to gene products that are involved in development in Drosophila and in oncogenesis in human cells. The cloned protein expressed in Escherichia coli has been purified and crystallized in a hexagonal space group with a = b = 74.9 A, c = 211.4 A. The asymmetric unit contains either one or two 17,000 Mr subunits of the hexamer.
authors.affiliation: Laboratoire de Biologie Physicochimique, Université Paris-Sud, Orsay, France.
authors.forename: C
authors.initials: C
authors.lastname: Dumas
authors.forename: G
authors.initials: G
authors.lastname: Lebras
authors.forename: V
authors.initials: V
authors.lastname: Wallet
authors.forename: M L
authors.initials: ML
authors.lastname: Lacombe
authors.forename: M
authors.initials: M
authors.lastname: Véron
authors.forename: J
authors.initials: J
authors.lastname: Janin
mesh_terms: D003461:Crystallography; D004023:Dictyostelium / Q000201:enzymology*; D009701:Nucleoside-Diphosphate Kinase / Q000648:ultrastructure*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000648:ultrastructure; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D009701:Nucleoside-Diphosphate Kinase