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.