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牙龈卟啉单胞菌是一种能够引起牙周炎的口腔病原菌,能够分泌许多种蛋白酶.这些蛋白酶在获得营养、逃脱宿主免疫、粘连组织细胞和其它疾病进程中发挥了重要作用,被认为是牙周炎的重要致病因子.其中一种蛋白酶是巯基蛋白酶Tpr,它能够降解许多常见蛋白酶的底物,其活性受到营养状态和钙离子浓度的调节.本实验在大肠杆菌中表达得到Tpr蛋白,经多种方法纯化后筛选获得蛋白质晶体.通过X射线衍射实验收集到分辨率达到0.20 nm的衍射数据,并使用软件HKL2000进行了处理.这些数据为解析Tpr3维晶体结构奠定了基础.
Porphyromonas gingivalis is an oral pathogen that can cause periodontitis and secrete many proteases that play an important role in gaining nutrition, escaping host immunity, adhesion tissue cells and other diseases and are thought to be Periodontitis is one of the important causative factors.One of the proteases is the thiol protease Tpr, which can degrade many common protease substrate, its activity by the nutritional status and calcium ion concentration regulation.This experiment expressed in E. coli Tpr protein , Which were purified by several methods and then screened to obtain protein crystals.The diffraction data with a resolution of 0.20 nm were collected by X-ray diffraction analysis and processed with software HKL2000.These data provide the basis for the resolution of Tpr3-dimensional crystal structure.