Electron cryomicroscopy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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]].
+
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. (Crystallization perhaps the major obstacle to determination of structure by X-ray diffraction.)
* [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 23:56, 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. (Crystallization perhaps the major obstacle to determination of structure by X-ray diffraction.)



Electron cryo-microscopy, Cryo-electron microscopy and Cryo-EM redirect to this page.

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, Joel L. Sussman, Karsten Theis, Angel Herraez

Personal tools