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 precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1, b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.
Hassell
A M
AM
Department of Macromolecular Sciences, Smith Kline & French Laboratories, King of Prussia, Pennsylvania 19406.
Johanson
K O
KO
Goodhart
P
P
Young
P R
PR
Holskin
B P
BP
Carr
S A
SA
Roberts
G D
GD
Simon
P L
PL
Chen
M J
MJ
Lewis
M
M
D000595:Amino Acid Sequence; D002847:Chromatography, Agarose; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008401:Gas Chromatography-Mass Spectrometry; D006801:Humans; D007375:Interleukin-1 / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000302:isolation & purification*; D014961:X-Ray Diffraction
D007375:Interleukin-1; D011994:Recombinant Proteins