Abstract
Crystals of M. tuberculosis phosphopantetheine adenylyltransferase 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 2.00-Å resolution. The crystals belong to sp. gr. P32 and have the following unit-cell parameters: a = b = 106.47 Å, c = 71.32 Å, α = γ = 90°, β = 120°. The structure was solved by the molecular-replacement method. There are six subunits of the enzyme comprising a hexamer per asymmetric unit. The hexamer is a biologically active form of phosphopantetheine adenylyltransferase from M. tuberculosis.
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Original Russian Text © V.I. Timofeev, L.A. Chupova, R.S. Esipov, I.P. Kuranova, 2015, published in Kristallografiya, 2015, Vol. 60, No. 5, pp. 745–747.
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Timofeev, V.I., Chupova, L.A., Esipov, R.S. et al. Crystallization and preliminary X-ray diffraction study of phosphopantetheine adenylyltransferase from M. tuberculosis crystallizing in space group P32 . Crystallogr. Rep. 60, 682–684 (2015). https://doi.org/10.1134/S106377451505017X
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DOI: https://doi.org/10.1134/S106377451505017X