Purification, crystallization and preliminary crystallographic characterization of the caspase-recruitment domain of human Nod1.
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 A resolution. The crystals belong to space group P3(1) or P3(2), with unit-cell parameters a = b = 79.1, c = 80.9 A. Preliminary analysis indicates that there is one dimeric CARD molecule in the asymmetric unit.
Srimathi
Thiagarajan
T
Basic Science, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.
Robbins
Sheila L
SL
Dubas
Rachel L
RL
Seo
Jang Hoon
JH
Park
Young Chul
YC
D020169:Caspases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D006801:Humans; D053474:Nod1 Signaling Adaptor Protein / Q000737:chemistry* / Q000302:isolation & purification*; D017434:Protein Structure, Tertiary
C119067:NOD1 protein, human; D053474:Nod1 Signaling Adaptor Protein; D020169:Caspases