Open AccessCrystallization and preliminary X‐ray crystallographic studies of the PYD domain of human NALP3
Author(s) -
Bae Ju Young,
Park Hyun Ho
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111035937
Subject(s) - nalp3 , inflammasome , aim2 , crystallization , crystallography , materials science , chemistry , biochemistry , receptor , organic chemistry
The NALP3 inflammasome is a macromolecular complex that is responsible for the innate immune response against infection by bacterial and viral pathogens. The NALP3 inflammasome is composed of three protein components: NALP3, ASC and caspase 1. Interaction between NALP3 and ASC via PYD domains is critical for the assembly of the NALP3 inflammasome. In this study, human NALP3 PYD, corresponding to amino acids 3–110, was overexpressed in Escherichia coli using engineered C‐terminal His tags. NALP3 PYD was then purified to homogeneity and crystallized at 293 K. Finally, X‐ray diffraction data were collected to a resolution of 1.7 Å from a crystal belonging to the primitive monoclinic space group P 2 1 , with unit‐cell parameters a = 42.03, b = 60.14, c = 51.61 Å, β = 107.40°.