CRYSTALLOGRAPHIC ANALYSIS OF FERRIC IRON BINDING PROTEIN BY MAD

多波长反常色散(MAD)数据 将利用硒和铁的散射来确定 嗜血杆菌铁铁结合蛋白的结构研究 流感病毒。这种蛋白质对几种致病细菌和 是基于结构的药物设计的一个很有前途的目标。试图 用传统方法测定晶体结构已经得到了很好的应用 非常令人沮丧。铁的极强反常散射 Atom和结合的硒-蛋氨酸将使这成为一种理想 疯狂分阶段的候选人。晶体的衍射率为1.6E。

Multiwavelength anomalous dispersion (MAD) data using anomalous scattering from selenium and iron will be used to determine the structure of ferric iron binding protein (FBP) from Haemophilus influenzae. This protein is vital to several pathogenic bacteria and is a promising target of structure-based drug design. Attempts to determine the crystal structure by traditional methods have been extremely frustrating. Very strong anomalous scattering from the iron atom along with incorporated seleno-methionine will make this an ideal candidate for MAD phasing. The crystals diffract to 1.6 E resolution.