Open AccessCrystallographic studies of bovine beta2-microglobulin.
Author(s) -
Joseph W. Becker,
Jack A. Ziffer,
Gerald M. Edelman,
Bruce A. Cunningham
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.8.3345
Subject(s) - orthorhombic crystal system , beta 2 microglobulin , crystallography , chemistry , peptide sequence , molecule , crystallization , antibody , immunoglobulin light chain , homologous chromosome , resolution (logic) , microbiology and biotechnology , biology , biochemistry , crystal structure , immunology , gene , organic chemistry , artificial intelligence , computer science
Crystals of the bovine milk protein lactollin yield x-ray diffraction data extending to a resolution of 2.8 A. Lactollin is a bovine analogue of beta2-microglobulin, a protein that is homologous in amino acid sequence to the constant domains of immunoglobulins and is the light chain of the human and murine major histocompatability antigens. The protein crystallizes in the orthorhombic space group P2(1)2(1)2(1) with a = 77.4, b = 47.9, and c = 34.3 A. The unit cell parameters and physical chemical solution studies indicate that the molecule exists in the crystal and in solution as a single polypeptide chain of 12,000 daltons.