Cryo-EM Service and Support Whether you are purchasing a new system, or need services for an existing system, we have a variety of support options and plans. See options Life in Atomic Resolution Electron and cryo-electron microscopy stories and solutions about the advancement of...
因为单颗粒冷冻电镜厚积薄发的技术突破，结构生物学在2013年底经历了一场“分辨率革命 (resolution revolution) ”，从此几家欢喜几家愁。欢喜的是，之前许多让科学家们束手无策的生物大分子们纷纷被揭开了神秘面纱；愁的是，作为研究者，为伊消得人憔悴、蓦然回首却在灯火阑珊处的乐趣少了许多。但是科研永无止境。
本研究使用的三个主要的cryoEMPEM maps都与多克隆抗体(pAbs)结合。cryoEM质量较好(3.3- to 3.7-Å ),并且Fab区结合附近有着high local resolution。 作者分析了Rh.4O9 pAbC-1 cryoEMPEM地图(Fig 1 left),Rh.4O9 与抗原的V1 loop相结合。有科学家从相同的恒河猴中分离出了同样识别这一表位的两个抗体...
Cryo-electron microscopy (cryo-EM) is advancing structural virology in instances where purifying virus proteins is a challenge, protein homogeneity is difficult to achieve, and image averaging may be the only way to obtain structural information at high resolution. These structural insights are revoluti...
目前的Cryo-EM主要分为了三个不同但密切相关的方向:电子晶体学(electron crystallography),单粒子冷冻电镜(single-particle cryo-EM)和电子低温断层扫描(electron cryotomography,Cryo-ET)。在过去几年中,单粒子Cryo-EM引发了结构生物学的革命,并已成为一个新的主导学科。
【人物】冷冻电镜(cryo-EM)顶级泰斗理查德·亨德森Richard Henderson 人物背景 理查德·亨德森(Richard Henderson),剑桥MRC分子生物学实验室教授,苏格兰人,生于1945年。1983年,年仅38岁的Henderson当选英国皇家学会院士。2016年,英国皇家学会决定将当年...
Structure-based designs facilitate drug discovery, and cryogenic electron microscopy (cryo-EM) is an increasingly important tool to determine high-resolution structures of proteins and protein complexes. This is especially true for certain classes ofproteins that have proven difficult to crystallize.The ...
Single particle cryo em is a powerful structural biology technique for 3D characterization of proteins, protein complexes and macromolecules at near-atomic and atomic resolution.
但是cryo-EM和其他材料电镜不同的是,我们希望能够移动和倾斜样品。因此我们需要个sample stage,而且必须非常精确。 可以在三维(XYZ)方向移动。需要非常精确,尤其是Z方向的移动关系到focus; 能够进行Tilt(cryo-ET常用),具有测角器(goniometer)。而且需要保证on-axis rotation; 在液氮温度下运行,收集高分辨率数据时其...
Electron cryo-microscopy (cryo-EM) single-particle analysis has yielded protein structures with increasing levels of detail in recent years1,2. However, it has proved difficult to obtain cryo-EM reconstructions with sufficient resolution to visualize individual atoms in proteins. Here we use a new ...