title: Crystallization and preliminary X-ray analysis of 4-pyridoxolactonase from Mesorhizobium loti.
abstract: 4-pyridoxolactonase from Mesorhizobium loti MAFF303099 has been overexpressed in Escherichia coli. The recombinant enzyme was purified and was crystallized by the sitting-drop vapour-diffusion method using PEG 4000 and ammonium sulfate as precipitants. Crystals of the free enzyme (form I) and of the 5-pyridoxolactone-bound enzyme (form II) grew under these conditions. Crystals of form I diffracted to 2.0 A resolution and belonged to the monoclinic space group C2, with unit-cell parameters a = 77.93, b = 38.88, c = 81.60 A, beta = 117.33 degrees. Crystals of form II diffracted to 1.9 A resolution and belonged to the monoclinic space group C2, with unit-cell parameters a = 86.24, b = 39.35, c = 82.68 A, beta = 118.02 degrees. The calculated V(M) values suggested that the asymmetric unit contains one molecule in both crystal forms.
authors.affiliation: Faculty of Agriculture, Graduate School of Integral Arts and Science, Kochi University, Monobe, Nankoku, Kochi, Japan.
authors.forename: Sayoko
authors.initials: S
authors.lastname: Matsuda
authors.forename: Nana
authors.initials: N
authors.lastname: Yokochi
authors.forename: Yu
authors.initials: Y
authors.lastname: Yoshikane
authors.forename: Jun
authors.initials: J
authors.lastname: Kobayashi
authors.forename: Chu Nhat
authors.initials: CN
authors.lastname: Huy
authors.forename: Seiki
authors.initials: S
authors.lastname: Baba
authors.forename: Seiki
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: Bunzo
authors.initials: B
authors.lastname: Mikami
authors.forename: Toshiharu
authors.initials: T
authors.lastname: Yagi
mesh_terms: D020561:Alphaproteobacteria / Q000201:enzymology*; D055162:Biocatalysis; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel
chemical_list: C050712:4-pyridoxolactonase; D002265:Carboxylic Ester Hydrolases