Abstract
Crystals of E. coli purine nucleoside phosphorylase were grown in microgravity by the capillary counter-diffusion method through a gel layer. The X-ray diffraction data set suitable for the determination of the three-dimensional structure at atomic resolution was collected from one crystal at the Spring-8 synchrotron facility to 0.99 Å resolution. The crystals belong to sp. gr. P21 and have the following unit-cell parameters: a = 74.1 Å, b = 110.2 Å, c = 88.2 Å, α = γ = 90°, β = 111.08°. The crystal contains six subunits of the enzyme comprising a hexamer per asymmetric unit. The hexamer is the biological active form of E. coli. purine nucleoside phosphorylase.
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Original Russian Text © Yu.A. Abramchik, V.I. Timofeev, N.E. Zhukhlistova, T.I. Muravieva, R.S. Esipov, I.P. Kuranova, 2015, published in Kristallografiya, 2015, Vol. 60, No. 4, pp. 575–578.
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Abramchik, Y.A., Timofeev, V.I., Zhukhlistova, N.E. et al. Purification, crystallization, and preliminary X-ray diffraction study of purine nucleoside phosphorylase from E. coli . Crystallogr. Rep. 60, 521–524 (2015). https://doi.org/10.1134/S1063774515040021
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DOI: https://doi.org/10.1134/S1063774515040021