Gorga J C, Madden D R, Prendergast J K, Wiley D C, Strominger J L
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Proteins. 1992 Jan;12(1):87-90. doi: 10.1002/prot.340120110.
The class I major histocompatibility (MHC) antigen HLA-B27 was purified by immunoaffinity chromatography from the homozygous human B lymphoblastoid cell line LG-2. Detergent-soluble HLA-B27 was cleaved with the protease papain to remove the hydrophobic transmembrane region and the cytoplasmic tail. Crystals of the resulting water-soluble extracellular fragments were obtained in hanging drops by the vapor-diffusion method. The crystals are triclinic, space group P1, with unit cell dimensions a = 45.9 A, b = 71.0 A, c = 83.7 A, alpha = 79.4 degrees, beta = 88.5 degrees, gamma = 89.9 degrees, and diffract beyond 2.5 A resolution.
