title: Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli.
abstract: L-Asparaginase is an enzyme which hydrolyzes asparagine to produce aspartic acid and ammonia. It is an effective chemotherapeutic drug, especially in the treatment of acute lymphoblastic leukaemia in children. The enzyme from Escherichia coli was crystallized in a new crystal form with space group C2, unit-cell parameters a = 76.3 (0), b = 134.6 (2), c = 64.8 (7) A, beta = 110.5 (1) degrees and a dimer in the asymmetric unit. Synchrotron-radiation diffraction data have been collected to 1.95 A resolution.
authors.affiliation: Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, CEP 13083-970, Campinas SP, Brazil. igor@lnls.br
authors.forename: I
authors.initials: I
authors.lastname: Polikarpov
authors.forename: R T
authors.initials: RT
authors.lastname: de Oliveira
authors.forename: J
authors.initials: J
authors.lastname: Abrahão-Neto
mesh_terms: D001215:Asparaginase / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D017356:Synchrotrons; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D001215:Asparaginase