Complex assembly, crystallization and preliminary X-ray crystallographic studies of MHC H-2Kd complexed with an HBV-core nonapeptide

In order to establish a system for structural studies of the murine class I major histocompatibility antigen complex (MHC) H-2K(d), a bacterial expression system and in vitro refolding preparation of the complex of H-2K(d) with human beta(2)m and the immunodominant peptide SYVNTNMGL from hepatitis B virus (HBV) core-protein residues 87 - 95 was employed. The complex ( 45 kDa) was crystallized; the crystals belong to space group P222(1), with unit-cell parameters a = 89.082, b = 110.398, c = 47.015 Angstrom, alpha = beta = gamma = 90degrees. The crystals contain one complex per asymmetric unit and diffract X-rays to at least 2.06 Angstrom resolution. The structure has been solved by molecular replacement and is the first crystal structure of a peptide - H-2K(d) complex.