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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

  • 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
  • Russian Academy of Sciences
  • Shubnikov Institute of Crystallography, Russian Academy of Sciences
  • Hauptman-Woodward Medical Research Institute, Inc.

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)629-634
Number of pages6
JournalCrystallography Reports
Volume47
Issue number4
DOIs
StatePublished - 2002

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