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 language | English |
|---|---|
| Pages (from-to) | 629-634 |
| Number of pages | 6 |
| Journal | Crystallography Reports |
| Volume | 47 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2002 |
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