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