Abstract
Ribokinase from a thermophilic strain of Thermus species 2.9 belonging to the carbohydrate ribokinase family (EC 2.7.1.15) was isolated, purified, and crystallized. The crystallization conditions were found by the vapor-diffusion technique and were then optimized to apply the capillary counter-diffusion technique. The X-ray diffraction data set was collected from the crystals, which were grown by the counter-diffusion technique, at the SPring-8 synchrotron radiation facility to 2.87 Å resolution. The crystals belong to sp. gr. P1211 and have the following unit-cell parameters: a = 81.613 Å, b = 156.132 Å, c = 87.714 Å, α = γ = 90°, β = 103.819°. The X-ray diffraction data set is suitable for determining the three-dimensional structure of the protein by the molecular-replacement method.
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Original Russian Text © Yu.A. Abramchik, V.I. Timofeev, T.I. Muravieva, R.S. Esipov, I.P. Kuranova, 2016, published in Kristallografiya, 2016, Vol. 61, No. 6, pp. 940–944.
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Abramchik, Y.A., Timofeev, V.I., Muravieva, T.I. et al. Crystallization and preliminary X-ray diffraction study of recombinant ribokinase from Thermus Species 2.9. Crystallogr. Rep. 61, 974–978 (2016). https://doi.org/10.1134/S106377451606002X
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DOI: https://doi.org/10.1134/S106377451606002X