EXPRESSION, PURIFICATION, CRYSTALLIZATION AND CRYSTALLOGRAPHIC CHARACTERIZATION OF THE HUMAN MHC CLASS-I RELATED PROTEIN MICA

Authors
BAUER S WILLIE ST SPIES T STRONG RK
Citation
S. Bauer et al., EXPRESSION, PURIFICATION, CRYSTALLIZATION AND CRYSTALLOGRAPHIC CHARACTERIZATION OF THE HUMAN MHC CLASS-I RELATED PROTEIN MICA, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 451-453
Citations number
17
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
3
Pages
451 - 453
Database
ISI
SICI code
0907-4449(1998)54:<451:EPCACC>2.0.ZU;2-Z
Abstract
Crystals of the human MHC-encoded molecule MICA, a homologue of MHC cl ass I proteins, have been grown in hanging-drop vapor-diffusion trials using ammonium sulfate as a precipitating agent with recombinant prot ein expressed in a baculovirus-based system. Cryo-preserved crystals o f MICA belong to the cubic space group F4(1)32 with lattice constants a = b = c = 260.7 Angstrom and diffract to a resolution limit of 3.0 A ngstrom when cryo-preserved. These crystals do not diffract when handl ed conventionally.