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
Webinar: CryoEM for Industrial Crystallographers
Webinar: Future Directions in CryoEM
Webinar: CryoEM & microED at NIS
Starter Program Brochure
- Han, Y., Reyes, A. A., Malik, S., & He, Y. (2020). Cryo-EM structure of SWI/SNF complex bound to a nucleosome. Nature, 579(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 America, 117(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. Nature, 27(3), 274–280. https://doi.org/10.1038/s41594-020-0386-8
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Speak with our experts about using Single Particle Analysis to support your drug discovery efforts.