title: Crystallographic studies of bovine beta2-microglobulin.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001609:Beta-Globulins; D002417:Cattle; D003126:Colostrum; D005260:Female; D006801:Humans; D007074:Immunoglobulin G; D007142:Immunoglobulin gamma-Chains; D008892:Milk; D008894:Milk Proteins; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011247:Pregnancy; D011487:Protein Conformation; D014357:Trypsin; D014961:X-Ray Diffraction; D001613:beta 2-Microglobulin
chemical_list: D001609:Beta-Globulins; D007074:Immunoglobulin G; D007142:Immunoglobulin gamma-Chains; D008894:Milk Proteins; D010446:Peptide Fragments; D001613:beta 2-Microglobulin; D014357:Trypsin