Crystallization of the complex of human IFN-gamma and the extracellular domain of the IFN-gamma receptor.
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.
Chène
C
C
Department of Pharmaceutical Research-New Technologies, F. Hoffmann-La Roche Ltd., Basel, Switzerland.
Fountoulakis
M
M
Döbeli
H
H
D'Arcy
B
B
Winkler
F
F
D'Arcy
A
A
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
D015703:Antigens, CD; D007371:Interferon-gamma; D017471:Receptors, Interferon; D011994:Recombinant Proteins; D000096743:Interferon gamma Receptor