Crystallization and preliminary X-ray diffraction studies of recombinant human interleukin-5.
Recombinant human interleukin-5 (rhIL-5) has been crystallized by the hanging drop vapor diffusion method using 0.1 M-Tris.HCl buffer (pH 8.5) containing 0.2 to 0.25 M-sodium acetate and 26 to 30% PEG 4000 at 22 degrees C. The parallel-piped crystals belong to the space group C2 with unit cell dimensions of a = 122.1 A, b = 36.11 A, c = 56.42 A, beta = 98.59 degrees. They diffract to at least 2.0 A resolution on a rotating anode X-ray source. The molecular mass weight of the protein and the volume of the unit cell suggest that the asymmetric unit contains one intermolecular disulfide-bonded homodimer.
Hassell
A M
AM
Glaxo Research Institute, Department of Structural and Biophysical Chemistry, Research Triangle Park, NC 27709.
Wells
T N
TN
Graber
P
P
Proudfoot
A E
AE
Anderegg
R J
RJ
Burkhart
W
W
Jordan
S R
SR
Milburn
M V
MV
D003460:Crystallization; D004926:Escherichia coli; D006801:Humans; D015848:Interleukin-5 / Q000737:chemistry*; D013058:Mass Spectrometry; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D015848:Interleukin-5; D011994:Recombinant Proteins