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- W2000220557 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." @default.
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- W2000220557 date "2011-09-30" @default.
- W2000220557 modified "2023-10-03" @default.
- W2000220557 title "Overexpression, crystallization and preliminary X-ray diffraction analysis of<scp>L</scp>-ribose isomerase from<i>Acinetobacter</i>sp. strain DL-28" @default.
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- W2000220557 doi "https://doi.org/10.1107/s1744309111030351" @default.
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