title: Crystallization of the complex of human IFN-gamma and the extracellular domain of the IFN-gamma receptor.
abstract: A complex of human interferon-gamma (IFN-gamma) with the soluble extracellular domain of the IFN-gamma receptor alpha-chain (IFN-gamma-R) has been crystallised. Crystals of the complex were grown using PEG 4000 as the precipitating agent in the presence of beta-octyl glucoside. The receptor-ligand complex crystallizes in a monoclinic space group and diffracts to about 3.0 A resolution. Isomorphous crystals have been obtained with complex containing selenomethionine and cysteine mutants of IFN-gamma, which may facilitate the ongoing X-ray structure determination.
authors: Department of Pharmaceutical Research-New Technologies, F. Hoffmann-La Roche Ltd., Basel, Switzerland.
authors: C
authors: C
authors: Chène
authors: M
authors: M
authors: Fountoulakis
authors: H
authors: H
authors: Döbeli
authors: B
authors: B
authors: D'Arcy
authors: F
authors: F
authors: Winkler
authors: A
authors: A
authors: D'Arcy
mesh_terms: D000595:Amino Acid Sequence; D015703:Antigens, CD / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D008027:Light; D013058:Mass Spectrometry; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D017471:Receptors, Interferon / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D012542:Scattering, Radiation; D000096743:Interferon gamma Receptor
chemical_list: D015703:Antigens, CD; D007371:Interferon-gamma; D017471:Receptors, Interferon; D011994:Recombinant Proteins; D000096743:Interferon gamma Receptor