Crystallization and preliminary X-ray crystallographic studies of cPOP1

The cellular pyrin domain-only protein 1 (cPOP1) was crystallized. The crystals were found to belong to the cubic space group P2₁3 with unit-cell parameters a = b = c = 94.12 Å, α = β = γ = 90.00°. The crystals were obtained at 293 K and diffracted to a resolution of 3.6 Å. Cellular pyrin domain-only protein 1 (cPOP1) is a pyrin domain (PYD)-containing protein that can regulate inflammation by preventing the assembly of inflammasome via direct interaction with ASC (apoptosis-associated speck-like protein containing a caspase recruitment domain). In this study, cPOP1, corresponding to amino acids 1–87, was overexpressed in Escherichia coli using an engineered C-terminal polyhistidine tag. cPOP1 was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 3.6 Å from a crystal belonging to the cubic space group P2₁3 with unit-cell parameters a = b = c = 94.12 Å, α = β = γ = 90.00°