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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / genetics
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Gene Expression
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H-2 Antigens / chemistry*
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H-2 Antigens / genetics
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H-2 Antigens / isolation & purification*
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HIV Envelope Protein gp160 / isolation & purification
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Histocompatibility Antigen H-2D
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Humans
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Mice
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Peptide Fragments / isolation & purification
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Protein Folding
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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beta 2-Microglobulin / isolation & purification
Substances
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H-2 Antigens
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HIV Envelope Protein gp160
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Histocompatibility Antigen H-2D
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Peptide Fragments
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Recombinant Proteins
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beta 2-Microglobulin