Crystallization and Preliminary Crystallographic Analysis of a TNF-β-55 kDa TNF Receptor Complex

A complex of tumour necrosis factor-β with the soluble extracellular domain of the human 55 kDa TNF receptor has been crystallized. Crystals of the complex were grown using polyethylene glycol 4000 as the precipitating agent in the presence of β-octyl glucoside. The receptor-ligand complex crystalli...

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Veröffentlicht in:	Journal of molecular biology 1993-01, Vol.229 (2), p.555-557
Hauptverfasser:	D'Arcy, Allan, Banner, David W., Janes, Wolfgang, Winkler, Fritz K., Loetscher, Hansruedi, Schönfeld, Hans-Joachim, Zulauf, Martin, Gentz, Reiner, Lesslauer, Werner
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Crystalline structure Crystallization cytokines Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Humans Lymphotoxin-alpha - chemistry Lymphotoxin-alpha - metabolism Molecular biophysics receptor Receptors, Cell Surface - chemistry Receptors, Cell Surface - metabolism Receptors, Tumor Necrosis Factor Structure in molecular biology TNF X-Ray Diffraction
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Zusammenfassung:	A complex of tumour necrosis factor-β with the soluble extracellular domain of the human 55 kDa TNF receptor has been crystallized. Crystals of the complex were grown using polyethylene glycol 4000 as the precipitating agent in the presence of β-octyl glucoside. The receptor-ligand complex crystallizes in a cubic space group and diffracts to 2·85 Å.
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.1993.1055