Abstract
HU proteins are involved in bacterial DNA and RNA repair. Since these proteins are absent in cells of higher organisms, inhibitors of HU proteins can be used as effective and safe antibiotics. The crystallization conditions for the M. gallisepticum HU protein were found and optimized by the vapor-diffusion method. The X-ray diffraction data set was collected to 2.91 Å resolution from the crystals grown by the vapor-diffusion method on a synchrotron source. The crystals of the HU protein belong to sp. gr. P41212 and have the following unit-cell parameters: a = b = 97.94 Å, c = 77.92 Å, α = β = γ = 90°.
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Original Russian Text © A.Yu. Nikolaeva, V.I. Timofeev, K.M. Boiko, D.A. Korzhenevskii, T.V. Rakitina, P.V. Dorovatovskii, A.V. Lipkin, 2015, published in Kristallografiya, 2015, Vol. 60, No. 6, pp. 922–925.
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Nikolaeva, A.Y., Timofeev, V.I., Boiko, K.M. et al. Isolation, purification, crystallization, and preliminary X-ray diffraction study of the crystals of HU protein from M. gallisepticum . Crystallogr. Rep. 60, 880–883 (2015). https://doi.org/10.1134/S1063774515060231
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DOI: https://doi.org/10.1134/S1063774515060231