title: Overproduction, crystallization and preliminary X-ray analysis of the putative L-ascorbate-6-phosphate lactonase UlaG from Escherichia coli.
abstract: UlaG, the putative L-ascorbate-6-phosphate lactonase encoded by the ulaG gene from the utilization of L-ascorbate regulon in Escherichia coli, has been cloned, overexpressed, purified using standard chromatographic techniques and crystallized. Crystals were obtained by sitting-drop vapour diffusion at 293 K. Preliminary X-ray diffraction analysis revealed that the UlaG crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 104.52, b = 180.69, c = 112.88 A, beta = 103.26 degrees. The asymmetric unit is expected to contain six copies of UlaG, with a corresponding volume per protein weight of 2.16 A3 Da(-1) and a solvent content of 43%.
authors: Structural Biology Department, Institut de Biologia Molecular de Barcelona and Institut de Recerca Biomèdica, E-08028 Barcelona, Spain.
authors: Fernando
authors: F
authors: Garces
authors: Francisco J
authors: FJ
authors: Fernández
authors: Rosa
authors: R
authors: Pérez-Luque
authors: Juan
authors: J
authors: Aguilar
authors: Laura
authors: L
authors: Baldomà
authors: Miquel
authors: M
authors: Coll
authors: Josefa
authors: J
authors: Badía
authors: M Cristina
authors: MC
authors: Vega
mesh_terms: D001483:Base Sequence; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D002265:Carboxylic Ester Hydrolases; C527649:L-ascorbate 6-phosphate lactonase, E coli; C019103:delta-lactonase