title: Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus.
abstract: Arylmalonate decarboxylase catalyses the enantioselective decarboxylation of alpha-aryl-alpha-methylmalonates to produce optically pure alpha-arylpropionates. The enzyme was crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction. X-ray diffraction data collected to a resolution of 3.0 A at cryogenic temperature showed that the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 83.13, b = 99.62, c = 139.64 A. This suggested that the asymmetric unit would contain between four and six molecules. Small-angle X-ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process.
authors.affiliation: Department of Physics, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Kanagawa 223-8522, Japan. nakasako@phys.keio.ac.jp
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Nakasako
authors.forename: Rika
authors.initials: R
authors.lastname: Obata
authors.forename: Ryosuke
authors.initials: R
authors.lastname: Okubo
authors.forename: Shyuichi
authors.initials: S
authors.lastname: Nakayama
authors.forename: Kenji
authors.initials: K
authors.lastname: Miyamoto
authors.forename: Hiromichi
authors.initials: H
authors.lastname: Ohta
mesh_terms: D000421:Alcaligenes / Q000201:enzymology*; D001426:Bacterial Proteins / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D002262:Carboxy-Lyases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D005615:Freezing; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D002262:Carboxy-Lyases; C071852:malonate decarboxylase