Purification, crystallization and preliminary crystallographic characterization of the caspase-recruitment domain of human Nod1

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106051955· OSTI ID:22360243

Srimathi, Thiagarajan; Robbins, Sheila L.; Dubas, Rachel L. ^[1]; Seo, Jang-Hoon ^[2]

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1. Basic Science, Fox Chase Cancer Center, Philadelphia, PA 19111 (United States)
2. Department of Clinical Laboratory Science, Shinheung College, Uijeongbu, Kyungki-Do 480-701 (Korea, Republic of)

The caspase-recruitment domain of the cytosolic pathogen receptor Nod1 was crystallized. X-ray diffraction data were collected to 1.9 Å resolution. 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 P3{sub 1} or P3{sub 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.

• OSTI ID: 22360243
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AFFINITY
CRYSTALLIZATION
CRYSTALS
ESCHERICHIA COLI
GELS
INTERACTIONS
MOLECULES
RECEPTORS
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION