cryo-EM Insights

What is cryo-EM?

Cryo-electron microscopy (cryo-EM) is a form of transmission electron microscopy (TEM) where samples are studied at cryogenic temperatures (typically liquid nitrogen temperatures). Cryo-EM is often used to determine the three-dimensional structures of biological molecules, such as proteins and nucleic acids. Samples are rapidly cooled to vitrify them, preserving their native state and preventing the formation of ice crystals that can damage the structure.

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What other technologies are related to cryo-EM?

cryo-EM Competitor Technologies

X-ray crystallography

X-ray crystallography is an alternative method for determining the atomic structure of molecules, particularly proteins. It competes with cryo-EM.

mentioned alongside cryo-EM in 36% (435) of relevant job posts

NMR

Nuclear Magnetic Resonance (NMR) spectroscopy is another method to determine the structure of molecules. In particular, NMR can be used to study protein dynamics and protein-ligand interactions and can thus serve as competitor to cryo-EM.

mentioned alongside cryo-EM in 1% (152) of relevant job posts

cryo-EM Complementary Technologies

ITC

Isothermal Titration Calorimetry (ITC) measures the heat released or absorbed during a binding event. It provides thermodynamic information, and is thus complementary, but provides no structural information.

mentioned alongside cryo-EM in 11% (98) of relevant job posts

SPR

Surface Plasmon Resonance (SPR) monitors biomolecular interactions in real time. It provides binding affinity data. While useful to characterize protein interactions, it doesn't provide structural information, thus complementary.

mentioned alongside cryo-EM in 4% (128) of relevant job posts

DSF

Differential Scanning Fluorimetry (DSF) assesses protein stability. It complements cryo-EM by helping to ensure sample quality, but provides no structural information.

mentioned alongside cryo-EM in 6% (52) of relevant job posts