Electron Microscopy

Cryo-EM in the Pharmaceutical Industry

See what your peers are saying about cryo-EM.

Since the beginning of the Resolution Revolution, there has been a growing enthusiasm for cryo-EM, and it shows no signs of stopping. Pioneering contributions to protein structure determination continue to roll out at an unprecedented pace. An increasing number of pharmaceutical companies are partnering with Thermo Fisher Scientific to realize the benefits of cryo-EM.

Most proteins of interest as drug targets are large, asymmetric, and act in complexes. Existing analytical techniques are limited to a subset of possible protein analytes. In fact, a minimal number of all structures in the Protein Data Bank (PDB) that were resolved by crystallography are complex structures composed of more than four chains. Cryo-EM enables high-resolution imaging of large protein complexes without crystallization, providing key information on drug targets and disease mechanisms.

 

See what your peers are saying about cryo-EM

"Cryo-EM is transforming structural biology, allowing us to study many target proteins for the first time and gain new mechanistic insights to help guide future drug design."

— Dr. Chris Phillips , Associate Director of Structural Biology, IMED Biotech Unit, AstraZeneca

"This represents a new era in imaging of proteins in humans with immense implications for drug design."

— Francis Collins, MD, PhD, NIH Director

"Cryo-EM is positioned to become an even more useful tool in structural biology and cancer drug development… This latest finding provides a tantalizing possibility for advancing effective drug development."

— Dr. Douglas Lowy , Director, USA National Cancer Institute

"Cryo-electron microscopy has really come on in leaps and bounds in the last few years. One of the requirements of X-ray crystallography is that you have to form crystals. With cryo-EM you don’t, which is a big advantage."

— Dr. Harren Jhoti , Founder, CEO, Astex Pharmaceuticals

"The requirement of X-ray crystallography is that you need to obtain a diffracting crystal to get atomic resolution. That has been a big hurdle if you’re working on challenging targets. Almost every target we’re working on now is very challenging."

— Dr. Seungil Han , Associate Research Fellow, Pfizer, Groton, CT

 

 
Style Sheet for Media Tabs
Cryo-EM Structure of HER2-trastuzumab-pertuzumab Complex&#x3b; Hao Y, Yu X, Bai Y, McBride HJ, Huang X (2019), PLoS ONE 14(5): e0216095, Published: May 1, 2019
Cryo-EM Structure of HER2-trastuzumab-pertuzumab Complex; Hao Y, Yu X, Bai Y, McBride HJ, Huang X (2019), PLoS ONE 14(5): e0216095, Published: May 1, 2019
Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin&#x3b; Xu et al., 2019, Cell 176, 702–715, Published: February 7, 2019
Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin; Xu et al., 2019, Cell 176, 702–715, Published: February 7, 2019
Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC polyomaviruses&#x3b; Lindner et al., 2019, Immunity 50, 668–676, 2019, Published: February 26, 2019
Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC polyomaviruses; Lindner et al., 2019, Immunity 50, 668–676, 2019, Published: February 26, 2019
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism, Nicholas G. Fox, et al., Nature Communications 10, Article number: 2210 (2019), Published: May 17, 2019
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism, Nicholas G. Fox, et al., Nature Communications 10, Article number: 2210 (2019), Published: May 17, 2019
Cryo-EM Structure of HER2-trastuzumab-pertuzumab Complex&#x3b; Hao Y, Yu X, Bai Y, McBride HJ, Huang X (2019), PLoS ONE 14(5): e0216095, Published: May 1, 2019
Cryo-EM Structure of HER2-trastuzumab-pertuzumab Complex; Hao Y, Yu X, Bai Y, McBride HJ, Huang X (2019), PLoS ONE 14(5): e0216095, Published: May 1, 2019
Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin&#x3b; Xu et al., 2019, Cell 176, 702–715, Published: February 7, 2019
Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin; Xu et al., 2019, Cell 176, 702–715, Published: February 7, 2019
Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC polyomaviruses&#x3b; Lindner et al., 2019, Immunity 50, 668–676, 2019, Published: February 26, 2019
Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC polyomaviruses; Lindner et al., 2019, Immunity 50, 668–676, 2019, Published: February 26, 2019
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism, Nicholas G. Fox, et al., Nature Communications 10, Article number: 2210 (2019), Published: May 17, 2019
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism, Nicholas G. Fox, et al., Nature Communications 10, Article number: 2210 (2019), Published: May 17, 2019

 

 

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