Also offered as gene-to-structure service.
Next-generation structure determination at near-atomic resolution
Protein structures from close-to-native conditions
Overcomes the need for crystallization
Highly suitable for larger proteins, complexes, and membrane proteins
Data collection requires access to high-end electron microscopes
Offers a unique opportunity to visualize proteins directly in an unperturbed cell
For difficult-to-extract/purify proteins in their native conformation, for example for membrane protein-ligand interactions
For the study of protein-protein interactions in a cellular context, for example for antibody-cell receptor interactions
For the study drug delivery vectors such as viral vectors, polymers, or nanoparticles
Highest resolutions (up to 1 Å and beyond)
Highly suitable for small, soluble proteins
Depends on crystallizability of the protein
Data collection requires coordinated access to high-energy X-ray sources (synchrotrons)
