Murine class I major histocompatibility complex H-2Dd:: expression, refolding and crystallization

A truncated soluble form of the murine class I major histocompatibility antigen complex H-2D(d) was cloned using an Escherichia coli based system. It was expressed, refolded in vitro and crystallized in a complex with murine beta(2) microglobulin and the peptide RGPGRAFVTI from the V3-loop of the gp160 HIV-1 protein. Crystals belonging to the space group P2(1)2(1)2(1) with cell dimensions a = 51.3, b = 92.5, c = 108.8 Angstrom were obtained using two different crystallization conditions. The crystals contain one complex per asymmetric unit and diffract to at least 2.4 Angstrom resolution.