Expression, purification, crystallization and crystallographic characterization of the human MHC class I related protein MICA
S Bauer, ST Willie, T Spies, RK Strong - … Crystallographica Section D …, 1998 - scripts.iucr.org
S Bauer, ST Willie, T Spies, RK Strong
Acta Crystallographica Section D: Biological Crystallography, 1998•scripts.iucr.orgCrystals 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 Å and diffract to a resolution limit of 3.0 Å when cryo-preserved. These crystals
do not diffract when handled conventionally.
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 Å and diffract to a resolution limit of 3.0 Å when cryo-preserved. These crystals
do not diffract when handled conventionally.
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 Å and diffract to a resolution limit of 3.0 Å when cryo-preserved. These crystals do not diffract when handled conventionally.
International Union of Crystallography