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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 |
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| Authors: | P V Afonin A V Fokin L N Shingarova V G Korobko I N Tsygannik I V Artem’ev S V Pletnev W Pangborn W L Duax V Z Pletnev |
| Institution: | (1) Shemyakin Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia;(2) Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, Moscow, 117333, Russia;(3) Hauptman-Woodward Medical Research Institute, 73 High Street, Buffalo, New York 14203-1196, USA |
| 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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