Publication Abstract from PubMed
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 A, beta = 118.16 degrees , and the orthorhombic space group F222, with unit-cell parameters a = 96.44, b = 106.26, c = 117.83 A. Diffraction data were collected to 3.1 and 2.2 A resolution, respectively.
Overexpression, crystallization and preliminary X-ray diffraction analysis of L-ribose isomerase from Acinetobacter sp. strain DL-28.,Yoshida H, Teraoka M, Yoshihara A, Izumori K, Kamitori S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1281-4., doi: 10.1107/S1744309111030351. Epub 2011 Sep 30. PMID:22102048[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
