Crystallization and preliminary X-ray analysis of the atrial natriuretic peptide (ANP) receptor extracellular domain complex with ANP: use of ammonium sulfate as the cryosalt.
Crystallization and preliminary X-ray analysis of the atrial natriuretic peptide (ANP) receptor extracellular domain complex with ANP: use of ammonium sulfate as the cryosalt.
复制标题
心房钠尿肽 (ANP) 受体胞外结构域与 ANP 复合物的结晶和初步 X 射线分析：使用硫酸铵作为冷冻盐。
DOI：
10.1107/s0907444903016445
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Misono,KunioS
中科院分区：
文献类型：
--
作者：
Ogawa,Haruo;Zhang,Xiaolun;Qiu,Yue;Ogata,CraigM;Misono,KunioS
心房利钠肽（ANP）由于其利钠和扩血管活性而在血压和容量调节中起主要作用。心钠素受体是一种与其内在鸟苷酸环化酶活性偶联的单跨膜受体。大鼠心钠素受体（ANPR）的胞外结合区的过表达在CHO细胞中的永久转染和纯化。用悬滴气相扩散法在301 K下结晶ANPR与ANP络合物。将晶体在用作冷冻保护剂的3.4M硫酸铵中冷冻。 晶体用同步辐射衍射到3.1 μ m分辨率，属于六方空间群P61，晶胞参数a = B = 100.3，c = 258.6 μ m。
Atrial natriuretic peptide (ANP) plays a major role in blood pressure and volume regulation owing to its natriuretic and vasodilatory activities. The ANP receptor is a single-span transmembrane receptor coupled to its intrinsic guanylyl cyclase activity. The extracellular hormone-binding domain of rat ANP receptor (ANPR) was overexpressed by permanent transfection in CHO cells and purified. ANPR complexed with ANP was crystallized at 301 K by the hanging-drop vapor-diffusion method. The crystals were frozen in 3.4 M ammonium sulfate used as a cryoprotectant. The crystals diffracted to 3.1 Å resolution using synchrotron radiation and belonged to the hexagonal space group P61, with unit-cell parameters a = b = 100.3, c = 258.6 Å.