Open AccessPurification, crystallization and preliminary crystallographic characterization of the caspase‐recruitment domain of human Nod1
Author(s) -
Srimathi Thiagarajan,
Robbins Sheila L.,
Dubas Rachel L.,
Seo JangHoon,
Park Young Chul
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106051955
Subject(s) - crystallization , characterization (materials science) , nod1 , domain (mathematical analysis) , crystallography , materials science , chemistry , nanotechnology , chemical engineering , biochemistry , engineering , receptor , mathematics , innate immune system , mathematical analysis , nod2
The caspase‐recruitment domain (CARD) is known to play an important role in apoptosis and inflammation as an essential protein–protein interaction domain. The CARD of the cytosolic pathogen receptor Nod1 was overexpressed in Escherichia coli and purified by affinity chromatography and gel filtration. The purified CARD was crystallized at 277 K using the microseeding method. X‐ray diffraction data were collected to 1.9 Å resolution. The crystals belong to space group P 3 1 or P 3 2 , with unit‐cell parameters a = b = 79.1, c = 80.9 Å. Preliminary analysis indicates that there is one dimeric CARD molecule in the asymmetric unit.