[ExI] Cryo–electron microscopy

John Clark johnkclark at gmail.com
Thu Oct 22 15:05:25 UTC 2020


If you know the shape of a protein you can figure out how it works, the
traditional way of doing it is to crystallize the protein and then use
x-ray diffraction, but many important proteins can't be crystallized such
as those in ribosomes and in cell membranes. An alternative method is
Cryo–electron microscopy, It involves flash freezing the protein and then
taking many electron microscope pictures of it from random angles and
stitching all that information together with software to make a 3-D
picture, but until now the resolution wasn't good enough to see individual
atoms. In the October 21, 2020 issue of Nature there is a report of a
Cryo–electron microscope that, thanks to an improved electron beam and
improved software, has a resolution of 1.25 * 10^-10 meters, and that's
good enough to see an individual hydrogen atom.  This should revolutionize
the study of proteins structure and their function.

Atomic-resolution protein structure determination by cryo-EM
<https://www.nature.com/articles/s41586-020-2833-4>


John K Clark
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