Expression, purification, crystallization and crystallographic characterization of the human MHC class I related protein MICA.
Crystals of the human MHC-encoded molecule MICA, a homologue of MHC class I proteins, have been grown in hanging-drop vapor-diffusion trials using ammonium sulfate as a precipitating agent with recombinant protein expressed in a baculovirus-based system. Cryo-preserved crystals of MICA belong to the cubic space group F4132 with lattice constants a = b = c = 260.7 A and diffract to a resolution limit of 3.0 A when cryo-preserved. These crystals do not diffract when handled conventionally.
Division of Clinical Research, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave N, Seattle, Washington, 98109-1024, USA.
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S
Bauer
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Willie
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Spies
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Strong
D003460:Crystallization; D018360:Crystallography, X-Ray; D015395:Histocompatibility Antigens Class I / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D006801:Humans; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification
D015395:Histocompatibility Antigens Class I; C099187:MHC class I-related chain A; D011994:Recombinant Proteins