Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

2.7K
Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
2.7K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.0K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
4.0K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Crystal structure determination of an Fe<sup>II</sup> azo aldehyde complex [Fe(C<sub>14</sub>H<sub>11</sub>N<sub>2</sub>O<sub>3</sub>)<sub>2</sub>(H<sub>2</sub>O)<sub>2</sub>] by MicroED.

Acta crystallographica. Section E, Crystallographic communications·2026
Same author

Structural and functional mapping of protective human monoclonal antibodies against enterovirus A71.

Science advances·2026
Same author

Affinity purification contaminants identified by cryo-EM and mass spectrometry.

Bioscience reports·2026
Same author

Structural basis of signal peptide recognition by the signal peptidase complex.

Nature communications·2026
Same author

Twelve phosphomimetic mutations induce the assembly of recombinant full-length human tau into paired helical filaments.

eLife·2026
Same author

Structural basis of Ku-mediated activation of WRN exonuclease activity.

Nature communications·2026

相关实验视频

Updated: Dec 4, 2025

Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

9.3K

在原子分辨率下单颗粒冷电磁波

Takanori Nakane1, Abhay Kotecha2, Andrija Sente1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

Nature
|October 22, 2020
PubMed
概括
此摘要是机器生成的。

新的冷电子显微镜 (cryo-EM) 技术实现了蛋白质结构的原子分辨率. 这一突破使得原子和键的详细可视化成为可能,

更多相关视频

Manual Blot-and-Plunge Freezing of Biological Specimens for Single-Particle Cryogenic Electron Microscopy
09:16

Manual Blot-and-Plunge Freezing of Biological Specimens for Single-Particle Cryogenic Electron Microscopy

Published on: February 7, 2022

7.0K
Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency
06:41

Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency

Published on: May 10, 2024

2.3K

相关实验视频

Last Updated: Dec 4, 2025

Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

9.3K
Manual Blot-and-Plunge Freezing of Biological Specimens for Single-Particle Cryogenic Electron Microscopy
09:16

Manual Blot-and-Plunge Freezing of Biological Specimens for Single-Particle Cryogenic Electron Microscopy

Published on: February 7, 2022

7.0K
Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency
06:41

Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency

Published on: May 10, 2024

2.3K

科学领域:

  • 结构生物学
  • 生物物理
  • 生物化学

背景情况:

  • 蛋白质结构决定生物功能.
  • 高分辨率的蛋白质结构对于理解分子机制至关重要.
  • 电子冷显微镜 (cryo-EM) 已经推进了蛋白质结构的确定.

研究的目的:

  • 使用冷电磁单粒子分析实现原子分辨率.
  • 为了可视化单个原子,溶剂分子和蛋白质中的键.
  • 实现基于结构的药物发现和高通量选.

主要方法:

  • 使用一种新的电子源,能量过器和冷电磁镜的摄像头.
  • 对人类膜蛋白 (β3 GABA受体) 和小鼠阿波费里丁进行单颗粒分析.
  • 开发了数据采集和样本准备的先进技术.

主要成果:

  • 获得了β3GABA受体的1. 7 Å分辨率的冷EM重建.
  • 实现了小鼠的1.22 Å分辨率,提供了原子分辨率的视图.
  • 在蛋白质结构中可视化原子及其结合网络.

结论:

  • 在冷电磁技术的进步使得常规的原子分辨率.
  • 这种分辨率水平有助于详细了解蛋白质的结构和功能.
  • 该方法支持小分子查和基于结构的药物发现.