Open AccessOverexpression, crystallization and preliminary X‐ray diffraction analysis of l ‐ribose isomerase from Acinetobacter sp. strain DL‐28
Author(s) -
Yoshida Hiromi,
Teraoka Misa,
Yoshihara Akihide,
Izumori Ken,
Kamitori Shigehiro
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111030351
Subject(s) - strain (injury) , crystallization , ribose , isomerase , x ray crystallography , crystallography , materials science , diffraction , microbiology and biotechnology , chemistry , biochemistry , biology , enzyme , physics , optics , organic chemistry , anatomy
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 C 2, with unit‐cell parameters a = 96.60, b = 105.89, c = 71.83 Å, β = 118.16°, and the orthorhombic space group F 222, 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.