Open AccessCrystallization and preliminary X‐ray crystallographic studies of cPOP1
Author(s) -
Do Kyung Hoon,
Park Hyun Ho
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113002686
Subject(s) - pyrin domain , inflammasome , crystallization , crystallography , escherichia coli , protein crystallization , chemistry , materials science , biochemistry , gene , receptor , organic chemistry
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 P 2 1 3 with unit‐cell parameters a = b = c = 94.12 Å, α = β = γ = 90.00°.