The power of Cryo-EM in Structural Biology

The resolution revolution in cryo-EM has made it possible for structural biologists to define the structures of individual proteins by using cryo-electron microscopy (Cryo-EM). A recent wave of technological improvements has led to a marked increase in the achievable resolution that ultimately enables the visualization of individual protein atoms in optimized samples. A resolution of 1.2Å was achieved with single particle cryo-EM (SPA) on a well-behaving Apoferritin sample providing a genuine atomic resolution view of such protein. Using these latest improvements the resolution for a challenging human membrane protein, the GABA_A receptor, was pushed to 1.7 Å. Such resolution provides unprecedented levels of detail and understanding of small molecule coordination.

These  breakthroughs in resolution were achieved by a combination of advances in software and new hardware on the Titan Krios such as a new cold-field emission gun and an ultra-stable Selectris™ energy filter in combination with the latest Falcon4 direct electron detector. These developments did not only push the resolution but also resulted in an increased throughput.

The new Selectris™energy filter also pushed the resolution on the more affordable 200 kV Glacios reaching a resolution of 1.7Å on Apoferritin and 2.4Å on the human GABA_A receptor.

With the new Tundra™ Cryo-TEM, more scientists can have access to the revolutionary cryo electron microscopy technique with a cost effective, easy-to-use cryo-transmission electron microscope. Using the same cryo-infrastructure and an optimized objective lens the new Tundra reaches results that allow to study protein-protein interactions and model building.

In this presentation, we will discuss the latest developments in cryo-electron microscopy and share some exciting results from the new Selectris™ Imaging Filter and the new Tundra™ Cryo-TEM.