Preliminary X-ray crystallography studies of recombinant human interleukin-1 alpha. Purification and structural characterization

Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method using dimethyl sulfoxide as the precip...

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Veröffentlicht in:	The Journal of biological chemistry 1989-03, Vol.264 (9), p.4948-4952
Hauptverfasser:	Hassell, A M, Johanson, K O, Goodhart, P, Young, P R, Holskin, B P, Carr, S A, Roberts, G D, Simon, P L, Chen, M J, Lewis, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Chromatography, Agarose Chromatography, DEAE-Cellulose Chromatography, Gel Electrophoresis, Polyacrylamide Gel Gas Chromatography-Mass Spectrometry Humans Interleukin-1 - isolation & purification Isoelectric Focusing man Molecular Sequence Data Recombinant Proteins - isolation & purification X-Ray Diffraction
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