Abstract
Recombinant purine nucleoside phosphorylase from the thermophilic Thermus thermophilus strain encoded by the TT_C0194 gene was purified to homogeneity. The crystallization conditions for the enzyme were found by the vapor-diffusion technique. The crystals of the enzyme suitable for X-ray diffraction were grown under microgravity conditions by the capillary counter-diffusion method. The crystals belong to sp. gr. P212121 and have the following unit-cell parameters: a = 89.9 Å, b = 121.0 Å, c = 215.7 Å, α = β = γ = 90°. The X-ray diffraction data set suitable for the determination of the three-dimensional structure of purine nucleoside phosphorylase was collected from the grown crystals at the SPring-8 synchrotron facility to 2.5 Å resolution.
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Original Russian Text © E.V. Sinitsyna, V.I. Timofeev, N.E. Zhukhlistova, T.I. Muravieva, M.A. Kostromina, R.S. Esipov, I.P. Kuranova, 2018, published in Kristallografiya, 2018, Vol. 63, No. 5, pp. 742–745.
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Sinitsyna, E.V., Timofeev, V.I., Zhukhlistova, N.E. et al. Crystallization and Preliminary X-ray Diffraction Study of Purine Nucleoside Phosphorylase from the Thermophilic Bacterium Thermus thermophilus Strain HB27. Crystallogr. Rep. 63, 761–764 (2018). https://doi.org/10.1134/S1063774518050279
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DOI: https://doi.org/10.1134/S1063774518050279