High Resolution Protein Structures

Single particle analysis by cryoEM has advanced tremendously with improvements in electron microscopes, detectors, computation and sample preparation. The method now provides high resolution protein structures comparable to those determined by X-ray crystallography. 


At NIS, we have delivery data for over 200 high resolution data sets since June 2017. These have structurally enabled Drug Discovery pipelines for:

  • Integral membrane proteins, including ion channels, transporters, and GPCRs
  • large protein complexes
  • molecular machines & dynamic systems
  • gene editors

Our robust workflow supports the full range of cryoEM support from sample characterization via negative stain through 3D reconstruction, with more than 70% of structures determined from Krios-generated data achieving resolutions better than 3.5A. Sample preparation and optimized data acquisition strategies ensure reproducible protocols for ligand iterations to support medicinal chemistry programs using structure-based drug design.

NIS services have been designed to support a full range of projects from early proof-of-concept studies to long term sustainable access to instrumentation and FTE resource, allowing Pharma and Biotech clients to rapidly expand their SBDD target enablement programs.


Useful Resources

  • Han, Y., Reyes, A. A., Malik, S., & He, Y. (2020). Cryo-EM structure of SWI/SNF complex bound to a nucleosome. Nature579(7799), 452–455. https://doi.org/10.1038/s41586-020-2087-1
  • Kumar, P., Wang, Y., Zhang, Z., Zhao, Z., Cymes, G. D., Tajkhorshid, E., & Grosman, C. (2020). Cryo-EM structures of a lipid-sensitive pentameric ligand-gated ion channel embedded in a phosphatidylcholine only bilayer. Proceedings of the National Academy of Sciences of the United States of America117(3), 1788–1798. https://doi.org/10.1073/pnas.1906823117​​​​​​​​​​​​​​​​​​​
  • Kobayashi, K., Shihoya, W., Nishizawa, T., Kadji, F. M. N., Aoki, J., Inoue, A., & Nureki, O. (2020). Cryo-EM structure of the human PAC1 receptor coupled to an engineered heterotrimeric G protein. Nature27(3), 274–280. https://doi.org/10.1038/s41594-020-0386-8

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