DATA COLL FROM WEAKLY DIFFRACTING, ANISOTROPIC & RADIATION SENSITIVE CRYSTALS

弱衍射、各向异性数据采集

• 批准号: 6119483
• 负责人: SRIDHAR G PRASAD
• 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/6119483
• 关键词: biomaterials; genome; proteins

The energy-transducing nicotinamide transhydrogenases (THs) of mammalian and bacteria are structurally related membrane-bound enzymes that catalyze the direct transfer of a hydride ion between NAD(H) and NADP(H) in a reaction coupled to transmembrane proton translocation. The NADPH produced by TH is to reduce H2O2, which is capable of causing oxidative damage to intramitochondrial DNA and proteins, and initiating lipid peroxidation. Therefore, in order to understand the proton translocation mechanism and the reaction catalyzed by these enzymes a detailed knowledge of their three dimensional structure is essential. Weakly diffracting, highly anisotropic and radiation sensitve crystals of the alfa-1 subunit of R. rubrum TH have been obtained. These crystals diifract only to 4 E resolution using in-house x-ray source, whereas, the same crystals diffract to 2.7 E on BL7-1.

的能量转导烟酰胺转氢酶（TH）， 哺乳动物和细菌是结构上相关的膜结合酶 其催化NAD（H）和NAD（H）之间的氢化物离子的直接转移， NADP（H）在与跨膜质子易位偶联的反应中。 TH产生的NADPH是还原H2 O2，H2 O2能够 对线粒体内DNA和蛋白质造成氧化损伤， 引发脂质过氧化。 因此，为了了解 质子转移机理及其催化的反应 酶的三维结构的详细知识， 具有本质意义 弱衍射、高度各向异性和辐射 α-1亚基的敏感晶体。红色TH已被 得到了 这些晶体衍射只有4 E分辨率使用 内部的x射线源，而相同的晶体在2.7 E的作用下， BL7-1