200keV Transmission Cryo-Electron Microscope

BZR的研究重点是通过利用结构生物学工具箱，包括电子显微镜，核磁共振和x射线晶体学，全面了解分子蛋白质的功能。BZR的研究得到了随后几个dfg授予的关于大核糖核蛋白复合物结构/功能（CRC 960）和肾脏研究（CRC 699）的协调项目的支持。正在进行的研究集中在真核生物和古细菌的蛋白质/蛋白质- dna或-RNA复合物和膜蛋白上，它们代表了结构确定的挑战性目标。几个研究小组在构象动态蛋白质复合物的生产和表征以及通过新兴的低温电镜单颗粒分析技术确定结构方面积累了杰出的专业知识，该技术只需要少量的纯蛋白质，同时保留了潜在的构象异质性，这将是破译分子机制的最终下一步。与国外冷冻电镜核心设施的合作表明，由于(1)目标蛋白质的脆弱性需要现场冷冻保存优化，(2)项目数量不断增加，无法在远程模式下进行竞争性数据收集。为了保持国际竞争力，生物物理II系-结构生物学-与CRC 960一起计划在BZR建立一个自动化的高分辨率低温电子显微镜设备，专门用于单粒子分析和（串行）微晶体电子衍射的开发，后者与物理学院合作。

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.