PRELIMINARY-X-RAY CRYSTALLOGRAPHY STUDIES OF RECOMBINANT HUMAN INTERLEUKIN-1-ALPHA - PURIFICATION AND STRUCTURAL CHARACTERIZATION

  • 25 March 1989
    • journal article
    • research article
    • Vol. 264  (9) , 4948-4952
Abstract
Human interleukin-1.alpha., cloned and expressed in Escherichia 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 precipitating agent. The space group is P212121. Unit cell dimensions are a = 44.1, b - 57.1, and c = 61.7 .ANG. and .alpha. = .beta. = .gamma. = 90.degree.. The crystals diffract to beyond 1.7 .ANG. and are suitable for high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.