Crystallographic structure studies of an IgG molecule and an Fc fragment

@article{Huber1976CrystallographicSS,
  title={Crystallographic structure studies of an IgG molecule and an Fc fragment},
  author={R. Huber and J. Deisenhofer and P. Colman and M. Matsushima and W. Palm},
  journal={Nature},
  year={1976},
  volume={264},
  pages={415-420}
}
  • R. Huber, J. Deisenhofer, +2 authors W. Palm
  • Published 1976
  • Chemistry, Medicine
  • Nature
  • The crystal structures of a human IgG antibody molecule Kol and a human Fc fragment have been determined at 4-Å and 3.5-Å resolution respectively, by isomorphous replacement. The electron-density maps were interpreted in terms of immunoglobulin domains based on the Rei and McPC 603 models (Kol) and by model-building (Fc). The Fab parts of Kol have a different quaternary structure from that observed in isolated crystalline Fab fragments, there being no longitudinal V–C contact in Kol. The Fc… CONTINUE READING
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