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Expression, purification, crystallization and crystallographic characterization of the human MHC class I related
1Division of Clinical Research, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave N, Seattle, Washington, 98109-1024, USA.
Acta Crystallographica. Section D, Biological Crystallography
|October 8, 1998
Abstract:
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.