title: Overexpression, crystallization and preliminary X-ray diffraction analysis of L-ribose isomerase from Acinetobacter sp. strain DL-28.
abstract: Acinetobacter sp. L-ribose isomerase (L-RI) catalyzes a reversible isomerization reaction between L-ribose and L-ribulose. To date, information on L-RI remains limited and its amino-acid sequence shows no similarity to those of any known enzymes. Here, recombinant His-tagged L-RI was successfully overexpressed, purified and crystallized. Crystals of His-tagged L-RI were obtained by the hanging-drop vapour-diffusion method at room temperature as two crystal forms which belonged to the monoclinic space group C2, with unit-cell parameters a = 96.60, b = 105.89, c = 71.83 Å, β = 118.16°, and the orthorhombic space group F222, with unit-cell parameters a = 96.44, b = 106.26, c = 117.83 Å. Diffraction data were collected to 3.1 and 2.2 Å resolution, respectively.
authors.affiliation: Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Kita-gun, Kagawa 761-0795, Japan.
authors.forename: Hiromi
authors.initials: H
authors.lastname: Yoshida
authors.forename: Misa
authors.initials: M
authors.lastname: Teraoka
authors.forename: Akihide
authors.initials: A
authors.lastname: Yoshihara
authors.forename: Ken
authors.initials: K
authors.lastname: Izumori
authors.forename: Shigehiro
authors.initials: S
authors.lastname: Kamitori
mesh_terms: D000150:Acinetobacter / Q000201:enzymology*; D019747:Aldose-Ketose Isomerases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray
chemical_list: D019747:Aldose-Ketose Isomerases; C022546:ribose isomerase
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