The structure of tumor necrosis factor-α at 2.6 Å resolution: Implications for receptor binding
MJ Eck, SR Sprang - Journal of Biological Chemistry, 1989 - ASBMB
The three-dimensional structure of tumor necrosis factor (TNF-α), a protein hormone
secreted by macrophages, has been determined at 2.6 Å resolution by x-ray crystallography.
Phases were determined by multiple isomorphous replacement using data collected from
five heavy atom derivatives. The multiple isomorphous replacement phases were further
improved by real space symmetry averaging, exploiting the noncrystallographic 3-fold
symmetry of the TNF-α trimer. An atomic model corresponding to the known amino acid …
secreted by macrophages, has been determined at 2.6 Å resolution by x-ray crystallography.
Phases were determined by multiple isomorphous replacement using data collected from
five heavy atom derivatives. The multiple isomorphous replacement phases were further
improved by real space symmetry averaging, exploiting the noncrystallographic 3-fold
symmetry of the TNF-α trimer. An atomic model corresponding to the known amino acid …