Time-critical structures for your project

Cryo-EM can help accelerate your drug design

Cryo-EM, comprised of a variety of techniques, including single particle analysis (SPA) and micro-electron diffraction (microED), is designed to determine the structures of proteins and small molecules. Using cryo-EM can help you increase the speed of your rational drug discovery and overcome your toughest structural chemistry challenges.

Cryo-EM can enable faster identification of best-in-class drugs by visualizing drug-target complexes, giving you key insight into the interactions of anything from small molecules to large macromolecular assemblies. By using single particle analysis, you can determine near-atomic level molecular structures, helping every compound reach its full potential, from hit to lead. Cryo-EM excels at exposing the structure of biologics as well, providing critical information for everything from therapeutic antibody epitope mapping to increasingly large biopharmaceuticals.

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Single particle analysis: No need for crystals

Single particle analysis vitrification (rapid plunge freezing) allows you to sidestep crystallization while facilitating protein purification. Because single particle analysis does not require sample crystallization or even recombinant overproduction, it is an incredibly versatile method that is well-suited for a wide range of targets, particularly membrane proteins and large assemblies in their native state. Our single particle analysis workflow combines cutting-edge hardware with dedicated automated sample screening software, allowing you to optimize your biochemistry and vitrification parameters before transferring your best samples to the cryo-transmission electron microscope (cryo-TEM) for the ultimate 3D structure analysis.

From protein sequence to structure

One of the greatest advantages of cryo-EM relative to conventional structural biology techniques is its ability to analyze large, complex and flexible structures. Often, these cannot be crystallized for X-ray crystallography (XRD) or are too large and complex for nuclear magnetic resonance (NMR) spectroscopy. These include many biologically important proteins, especially those with variable or flexible structures, such as membrane proteins. Our dedicated SPA workflow has been developed around our instruments to ensure a smooth pathway from sample preparation to image acquisition to data processing. This purpose-driven design can help a wider range of structural biology labs achieve faster time-to-data when determining the 3D structure of proteins and protein complexes at near-atomic resolution.

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Electron density map and molecular structure of Ebola secreted glycoprotein obtained with single particle analysis
Proteinase K structure and electron density map obtained with MicroED

MicroED: Structural chemistry with electrons

MicroED data is acquired using electrons instead of X-rays. Because of the stronger interaction of electrons with much smaller crystals, you can obtain a solvable structure from mere nanocrystals of your compound. Studies have also shown the potential for impressive time-to-structure results of just a few hours. This opens unheard of avenues of structural characterization for natural products, precious ligands and metabolites. Not only that, but microED also makes polymorph identification possible.

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Join the forefront of structural analysis

Cryo-EM is the ideal way to obtain time-critical information for your increasingly challenging targets, guiding the chemistry of compounds with the wildtype structure of membrane protein (GPCRs), nuclear factors, and multi-component complexes. No target is too big or complex; you can even see the binding mode between target and ligand. With cryo-EM, you can limit protein purification to a single step or use CRISPR-inserted affinity tags for endogenous purification.

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Electron density map of beta-galactosidase tetramer obtained with single particle analysis