Premium
Crystallization and preliminary X‐ray diffraction studies of the human major histocompatibility antigen HLA‐B27
Author(s) -
Gorga Joan C.,
Madden Dean R.,
Prendergast John K.,
Wiley Don C.,
Strominger Jack L.
Publication year - 1992
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340120110
Subject(s) - human leukocyte antigen , crystallization , histocompatibility , antigen , major histocompatibility complex , immunology , biology , chemistry , organic chemistry
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 P 1, with unit cell dimensions a = 45.9 Å, b = 71.0 Å, c = 83.7 Å, α = 79.4°, β = 88.5°, γ = 89.9°, and diffract beyond 2.5 Å resolution.