Purification, crystallization and preliminary crystallographic characterization of the caspase-recruitment domain of human Nod1
- Basic Science, Fox Chase Cancer Center, Philadelphia, PA 19111 (United States)
- 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, Vol. 63, Issue Pt 1; Other Information: PMCID: PMC2330101; PMID: 17183166; PUBLISHER-ID: bw5173; OAI: oai:pubmedcentral.nih.gov:2330101; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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