Purification, crystallization and preliminary crystallographic studies of the complex of interferon-lambda1 with its receptor.
Human interferon-lambda1 (IFN-lambda1(Ins)) and the extracellular domain of interferon-lambda1 receptor (IFN-lambda1R1) were expressed in Drosophila S2 cells and purified to homogeneity. Both IFN-lambda1(Ins) and interferon-lambda1 produced from Escherichia coli (IFN-lambda1(Bac)) were coupled with IFN-lambda1R1 at room temperature and the complexes were purified by gel filtration. Both complexes were crystallized; the crystals were flash-frozen at 100 K and diffraction data were collected to 2.16 and 2.1 A, respectively. Although the IFN-lambda1(Bac)-IFN-lambda1R1 and IFN-lambda1(Ins)-IFN-lambda1R1 complexes differed only in the nature of the expression system used for the ligand, their crystallization conditions and crystal forms were quite different. A search for heavy-atom derivatives as well as molecular-replacement trials are in progress.
Magracheva
Eugenia
E
Basic Research Program, SAIC-Frederick, Frederick, MD 21702, USA.
Pletnev
Sergei
S
Kotenko
Sergei
S
Li
Wei
W
Wlodawer
Alexander
A
Zdanov
Alexander
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004330:Drosophila; D006801:Humans; D007372:Interferons; D007378:Interleukins / Q000737:chemistry*; D017471:Receptors, Interferon / Q000737:chemistry*; D000095022:Interferon Lambda
D007372:Interferons; D007378:Interleukins; D017471:Receptors, Interferon; C000624353:interferon-lambda, human; D000095022:Interferon Lambda