Expression, purification and crystallization of fully active, glycosylated human interleukin-5.
Recombinant human interleukin-5 (hIL-5) has been expressed at high levels and produced in large quantities in baculovirus infected Sf9 insect cells. The glycosylated protein was purified using immuno-affinity chromatography and gel filtration. Purified hIL-5 has been crystallized using standard vapour diffusion techniques with PEG as a coprecipitant. The crystals belong to the C2 space group and diffract to 2 A.
Guisez
Y
Y
Roche Research Gent, Belgium.
Oefner
C
C
Winkler
F K
FK
Schlaeger
E J
EJ
Zulauf
M
M
Van der Heyden
J
J
Plaetinck
G
G
Cornelis
S
S
Tavernier
J
J
Fiers
W
W
D000818:Animals; D016367:Baculoviridae; D002460:Cell Line; D003001:Cloning, Molecular; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D015848:Interleukin-5 / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D008027:Light; D051379:Mice; D008819:Mice, Nude; D009036:Moths; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012542:Scattering, Radiation
D015848:Interleukin-5; D011994:Recombinant Proteins