200keV Transmission Cryo-Electron Microscope

BZR的研究重点是通过利用包括电子显微镜、核磁共振和X射线结晶学在内的结构生物学工具箱来全面了解分子蛋白质的功能。BZR研究通过DFG随后批准的关于大核糖核蛋白复合体结构/功能的几个协调方案(CRC960)和肾脏研究(CRC699)得到支持。正在进行的研究集中在真核和古生物蛋白质/蛋白质-DNA或-RNA复合体和膜蛋白上，这些都是结构确定的具有挑战性的目标。几个研究小组在构象动态蛋白质复合体的生产和表征以及通过新兴的低温EM单粒子分析技术确定结构方面积累了杰出的专业知识，这种技术只需要少量的纯蛋白质，同时保持潜在的构象异质性，将是破译分子机制的最终下一步。与国外冷冻-EM核心设施的合作表明，由于(1)需要现场冷冻保存优化的目标蛋白质的脆弱性，以及(2)项目数量的不断增加，无法以远程模式进行竞争性数据收集。为了保持国际竞争力，生物物理学II系-结构生物学系-与CRC960计划在BZR建立一个自动化的高分辨率低温EM设施，专门用于单粒子分析和(系列)微晶电子衍射的开发，后者与物理系合作。

Research at the BZR focuses on a holistic understanding of molecular protein function by exploiting structural biology toolbox including electron microscopy, NMR and X-ray crystallography. BZR research has been supported through several subsequent DFG-granted coordinated programmes on structure/function of large ribonucleoprotein complexes (CRC 960) and kidney research (CRC 699). On-going research concentrates on eukaryotic and archaeal protein/protein-DNA or -RNA complexes and membrane proteins, which represent challenging targets for structure determination. Several research groups built-up an outstanding expertise in the production and characterization of conformational dynamic protein complexes and structure determination by the emerging technique of cryo-EM single particle analysis that require only small amounts of pure protein while preserving potential conformational heterogeneity and will be the ultimate next step in order to decipher molecular mechanisms. Collaborations with cryo-EM core facilities abroad have demonstrated that competitive data collection cannot be performed in remote mode due to (1) the fragility of target proteins that require on-site cryo-preservation optimisation and (2) the constantly increasing number of projects. In order to stay internationally competitive, the department of Biophysics II- Structural Biology – together with the CRC 960 plans to establish an automated high-resolution cryo-EM facility at the BZR dedicated to single particle analysis and the development of (serial) micro-crystal electron diffraction, latter in collaboration with the Faculty of Physics.