Electron cryomicroscopy
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
{{stub}} | {{stub}} | ||
| - | Single-particle electron cryomicroscopy (cryo-EM) has become an important method for determining macromolecular structures. It is the basis for the [[Nobel Prizes for 3D Molecular Structure#2010-2019|2017 Nobel Prize in Chemistry]]. Although resolution is usually poorer than that obtained by [[X-ray crystallography]], cryo-EM has the great advantage of not requiring crystallization<ref> | + | Single-particle electron cryomicroscopy (cryo-EM) has become an important method for determining macromolecular structures. It is the basis for the [[Nobel Prizes for 3D Molecular Structure#2010-2019|2017 Nobel Prize in Chemistry]]. Although resolution is usually poorer than that obtained by [[X-ray crystallography]], cryo-EM has the great advantage of not requiring crystallization<ref>Obtaining highly-ordered crystals is perhaps the major obstacle to determination of structure by X-ray diffraction.</ref>. Cryo-EM is particularly |
* [https://www.youtube.com/watch?v=BJKkC0W-6Qk 3 min video] explaining the principles of cryo-EM. | * [https://www.youtube.com/watch?v=BJKkC0W-6Qk 3 min video] explaining the principles of cryo-EM. | ||
Revision as of 23:59, 1 January 2019
Single-particle electron cryomicroscopy (cryo-EM) has become an important method for determining macromolecular structures. It is the basis for the 2017 Nobel Prize in Chemistry. Although resolution is usually poorer than that obtained by X-ray crystallography, cryo-EM has the great advantage of not requiring crystallization[1]. Cryo-EM is particularly
- 3 min video explaining the principles of cryo-EM.
- 2017 Nobel laureate Richard Henderson explains the history of cryo-EM in this 5 min video.
Electron cryo-microscopy, Cryo-electron microscopy and Cryo-EM redirect to this page.
Notes and References
- ↑ Obtaining highly-ordered crystals is perhaps the major obstacle to determination of structure by X-ray diffraction.
