Abstract
The three-dimensional structure of the Arg32His mutant of the human tumor necrosis factor (TNF-α) was established at 2.5 Å resolution by the molecular replacement method. The crystals of the mutant belong to sp. gr. R3. The specimen has a hemihedral twinning fraction of approximately one half with the twin law corresponding to an additional twofold axis along the a-or b-axis of the crystal lattice. The model analysis of interactions between functionally important loop 29–36 of the mutant and the receptors p55 and p75 was performed.
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Translated from Kristallografiya, Vol. 47, No. 4, 2002, pp. 685–690.
Original Russian Text Copyright © 2002 by Afonin, Fokin, Shingarova, Korobko, Tsygannik, Artem’ev, S. Pletnev, Pangborn, Duax, V. Pletnev.
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Afonin, P.V., Fokin, A.V., Shingarova, L.N. et al. Three-dimensional structure of the Arg32His mutant of the human tumor necrosis factor determined at 2.5 Å resolution from X-ray data for a twin crystal. Crystallogr. Rep. 47, 629–634 (2002). https://doi.org/10.1134/1.1496062
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DOI: https://doi.org/10.1134/1.1496062