STAFF PRIORITY TIME CRYSTAL STRUCTURE OF E COLI RIBONUCLEASE I

大肠杆菌核糖核酸酶 I 的工作人员优先时间晶体结构

• 批准号: 6119370
• 负责人: HENRY BELLAMY
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119370
• 关键词: Fungi; biomaterials; genome; plants; proteins

We used our time on beamline 7-1 to collect data from E. coli ribonuclease I (RNase I), a base-nonspecific endoribonuclease. RNase I is a member of a widely distributed group of ribonucleases found in bacteria, fungi and plants. The gene for RNase I has been cloned and the enzyme has been subjected to site-directed mutagenesis. During this beamtime period we collected data to 2.0 E resolution from native crystals and Pt and U heavy-atom derivatives. In all cases the crystals were complexed with a DNA oligomer which is believed on chemical evidence to bind to the enzyme's active site. (We use DNA oligomers because RNA would be cut up by the enzyme). The data have been processed and have been used to calculate an electron density map. Refinement is in progress; as of now (Nov. '98) we have a 2.0 E resolution map with a crystallographic R factor of 22%. Refinement is continuing.

我们利用时间7-1在梁线上收集大肠杆菌的数据 核糖核酸酶I（RNase I），一种非特异性内核酸酶。 RNase 我是发现在 细菌，真菌和植物。 RNase I的基因被克隆了， 该酶已经过位置定向的诱变。 期间 在这个时期，我们将数据收集到2.0 e从天然 晶体和PT和U重原子衍生物。 在所有情况下 晶体与据信上的DNA低聚物复合 化学证据与酶的活性位点结合。 （我们使用DNA 低聚物是因为RNA会被酶切割）。 数据有 已处理并已用于计算电子密度 地图。 精炼正在进行中；截至目前（98年11月）我们有2.0 e 晶体学R系数的分辨率图为22％。 精致是 继续。