Electron Microscopy at BPS 2016.

I did my PhD on TRPV1. Before there was a TRPV1 structure. In fact, I defended my thesis about a week before I saw the first talk on the high resolution EM structure of TRPV1 by Yifan Cheng at the NIH in November 2013. After the talk, we were huddled around a bench in the lab, lively discussing what it all meant for us and our thought on TRPV1 when a PI from a neighboring lab came over and said, “Welcome to the beginning of the end of membrane protein crystallography.” It seemed extravagant at the time, but now, a little over two years later in Los Angeles, he wasn’t too far off. Electron Microscopy is increasingly a high resolution method, and watching its progress over the last couple years and its consequent presence at Biophysics has been staggering.

Saturday night at the ‘Cryo-EM Subgroup’ session Doreen Matthies showed a figure that elegantly showed this transformation (which she graciously shared with me for the purpose of this blog).


In Feb 2015, just a year after the beginning of the ‘Resolution Revolution‘ there were 56 EM structures with resolution below 4 Angstroms. In Feb 2016, at the time of this meeting, there were already 182 EM structures with resolution below 4 Angstroms. While, this is still small compared to the number of high resolution x-ray crystallography structures deposited in the same amount of time, the scientific impact and size of each of these structures is astounding to think of. The revolution has arrived!


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