Crystallization of the complex of human IFN‐γ and the extracellular domain of the IFN‐γ receptor

A complex of human interferon‐γ (IFN‐ γ) with the soluble extracellular domain of the IFN‐ γ receptor α‐chain (IFN‐γ‐R) has been crystallised. Crystals of the complex were grown using PEG 4000 as the precipitating agent in the presence of β‐octyl glucoside. The receptor‐ligand complex crystallizes i...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1995-12, Vol.23 (4), p.591-594
Hauptverfasser:	Chiène, Christiane, Fountoulakis, Michael, Döbeli, Heinz, D'Arcy, Brigitte, Winkler, Fritz, D'Arcy, Allan
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antigens, CD - chemistry Antigens, CD - isolation & purification Antigens, CD - metabolism Crystallization Crystallography, X-Ray cysteine mutants cytokines Humans IFN‐γ Interferon gamma Receptor Interferon-gamma - chemistry Interferon-gamma - isolation & purification Interferon-gamma - metabolism Light Mass Spectrometry Mutagenesis, Site-Directed Point Mutation receptor Receptors, Interferon - chemistry Receptors, Interferon - isolation & purification Receptors, Interferon - metabolism Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping Scattering, Radiation selenomethionine
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Zusammenfassung:	A complex of human interferon‐γ (IFN‐ γ) with the soluble extracellular domain of the IFN‐ γ receptor α‐chain (IFN‐γ‐R) has been crystallised. Crystals of the complex were grown using PEG 4000 as the precipitating agent in the presence of β‐octyl glucoside. The receptor‐ligand complex crystallizes in a monoclinic space group and diffracts to about 3.0 Å resolution. Isomorphous crystals have been obtained with complex containing selenomethionine and cysteine mutants of IFN‐γ, which may facilitate the ongoing X‐ray structure determination. © 1995 Wiley‐Liss, Inc.
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.340230415