Srimathi Thiagarajan, Robbins Sheila L, Dubas Rachel L, Seo Jang Hoon, Park Young Chul
Basic Science, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt 1):21-3. doi: 10.1107/S1744309106051955. Epub 2006 Dec 16.
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.
已知半胱天冬酶招募结构域（CARD）作为一种重要的蛋白质-蛋白质相互作用结构域，在细胞凋亡和炎症中发挥重要作用。胞质病原体受体Nod1的CARD在大肠杆菌中过表达，并通过亲和层析和凝胶过滤进行纯化。纯化后的CARD采用微量接种法在277 K下结晶。收集到分辨率为1.9 Å的X射线衍射数据。晶体属于空间群P3(1)或P3(2)，晶胞参数a = b = 79.1，c = 80.9 Å。初步分析表明，不对称单位中有一个二聚体CARD分子。
