Cryo-electron microscopy is ideal for large protein complexes, membrane proteins, and dynamic assemblies – cases where obtaining crystals is difficult. Our team employs high-resolution CryoEM to determine near-atomic-detail structures of such targets, expanding the range of druggable proteins. These CryoEM-derived 3D maps allow us to visualize protein–ligand interactions and inform structure-based drug design similarly to X-ray co-structures.
By integrating CryoEM into our platform, CrystalsFirst ensures no target is beyond reach. We combine advanced sample preparation with state-of-the-art imaging and processing pipelines to produce reliable structural data. The insights gleaned from CryoEM can be fed into our AI-driven drug discovery workflow (FragAI) just as crystallographic data are enabling design of novel inhibitors or degraders even for large complexes.
Our CryoEM capability, together with X-ray crystallography, provides a comprehensive structural biology toolkit. This means clients can count on high-quality structural insights for any target, accelerating the discovery of therapeutics against previously “undruggable” or complex biological systems.