title: Crystallization and preliminary X-ray diffraction studies of the human major histocompatibility antigen HLA-B27.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
authors.forename: J C
authors.initials: JC
authors.lastname: Gorga
authors.forename: D R
authors.initials: DR
authors.lastname: Madden
authors.forename: J K
authors.initials: JK
authors.lastname: Prendergast
authors.forename: D C
authors.initials: DC
authors.lastname: Wiley
authors.forename: J L
authors.initials: JL
authors.lastname: Strominger
mesh_terms: D002461:Cell Line, Transformed; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D015796:HLA-B27 Antigen / Q000737:chemistry*; D006801:Humans; D014961:X-Ray Diffraction
chemical_list: D015796:HLA-B27 Antigen