X-Ray Crystallographic Studies of the Fab and Fc Fragments of Human Myeloma Immunoglobulins

  1. R. J. Poljak,
  2. L. M. Amzel,
  3. H. P. Avey,
  4. L. N. Becka,
  5. D. J. Goldstein, and
  6. R. L. Humphrey
  1. Departments of Biophysics and Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland

This extract was created in the absence of an abstract.

Excerpt

Knowledge of the tertiary structure of immunoglobulins and their fragments should be of considerable interest in study of the antibody-antigen reaction and other aspects of the immune response. The availability of crystalline antibodies and immunoglobulins (Ig) and of specific crystalline fragments of these molecules opens the way for X-ray crystallographic investigations of their three-dimensional structures. Results of preliminary investigations on the Fc and Fab fragments carried out in this laboratory have been reported before (Poljak et al., 1967; Humphrey et al., 1969). In this paper we present our most recent results on the study of a Fab fragment and in particular on the search for isomorphous heavy atom substitutions and the refinement of heavy atom parameters which have enabled us to calculate an electron-density map of the Fab′ molecule at 6 Å resolution.

EXPERIMENTAL PROCEDURES

Fab New and Fab′ New (obtained by papain and pepsin fragmentation of myeloma IgG New,

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