Murine class I major histocompatibility complex H–2D^d: 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 β₂ microglobulin and the peptide RGPGRAFVTI from the V3-loop of the gp160 HIV-1 protein. Crystals belonging to the space group P2₁2₁2₁ with cell dimensions a = 51.3, b = 92.5, c = 108.8 Å were obtained using two different crystallization conditions. The crystals contain one complex per asymmetric unit and diffract to at least 2.4 Å resolution.