Human interferon-λ1 (IFN-λ1Ins) and the extracellular domain of interferon-λ1 receptor (IFN-1R1) were expressed in Drosophila S2 cells and purified to homogeneity. Both IFN-λ1 Ins and interferon-λ1 produced from Escherichia coli (IFN-λ1Bac) were coupled with IFN-λ1R1 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 Å, respectively. Although the IFN-λ1Bac-IFN-λ1R1 and IFN-λ1 Ins-IFN-λ1R1 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.
|Original language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|State||Published - Dec 25 2009|
All Science Journal Classification (ASJC) codes
- Structural Biology
- Condensed Matter Physics