Community Exclusive
Cryo-EM made easy by prof. Grant Jensen
Why care about cryo-EM?
The function of vast majority of proteins is critically dependent on their three-dimensional structure. Therefore, in order to really understand how the proteins function, we must know their structure at atomic level. For a long time, x-ray crystallography and nuclear magnetic resonance (NMR) were methods of choice for almost all obtained atomic resolution structures of proteins. The third method is cryo-electron microscopy (cryo-EM). This does not require crystals or labels and often proteins can be studied very close to physiological conditions. Although cryo-EM still suffers from a number of limitations, it is clearly a rapidly developing technique and in future might become method of choice for structure determination of most biomolecules.
Join the FEBS Network today
Joining the FEBS Network’s molecular life sciences community enables you to access special content on the site, present your profile, 'follow' contributors, 'comment' on and 'like' content, post your own content, and set up a tailored email digest for updates.
Professor, University of Latvia
