Published in
International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 1(55), p. 260-262, 1999
DOI: 10.1107/s0907444998005265
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Murine class I major histocompatibility complex H-2D(d): Expression, refolding and crystallization
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Robert A. Harris ,
Karina Persson,
Jonas Sundbäck,
Charles L. Sentman,
Gunter Schneider,
Ylva Lindqvist,
Klas Kärre
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Abstract
A truncated soluble form of the murine class I major histocompatibility antigen complex H-2Dd was cloned using an Escherichia coli based system. It was expressed, refolded in vitro and crystallized in a complex with murine beta2 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 A were obtained using two different crystallization conditions. The crystals contain one complex per asymmetric unit and diffract to at least 2.4 A resolution.