High Resolution Protein Structures

The importance of knowing the three-dimensional (3D) structure of proteins and protein-complexes has been well established: such knowledge allows for a deeper understanding of biological processes, mechanisms of action of molecules, and structure-activity relationships, and can inform all steps of drug design.  While historically X-ray crystallography and NMR have been the methods of choice for 3D structure determination,  single particle cryoEM has emerged as a complementary technique, especially for targets recalcitrant (because of size, stability, complexity and conformational variability) to the more standard structural techniques.


NIS is the first and only CRO services provider to own and operate the necessary hardware and software for full structure enablement from sample to final map production. Our growing fleet of in-house microscopes, combined with best-in-class IT infrastructure and scientific know-how, has supported over 200 SPA projects resulting in more than 60 unique protein structures, the vast majority of which have achieved resolutions of 3.5Å                                or better. Spanning large protein complexes to small integral membrane proteins, we've successfully tackled a diverse set of projects that would otherwise have lacked the structural information necessary to support medicinal chemistry and biologics development efforts.  


NIS provides a unique service offering that melds traditional CRO service packages with training and instrument access opportunities typically only accessible through academic and national laboratory facilities. In addition to project-based proposals, NIS offers custom service packages, onsite training in sample preparation and data acquisition, and data acquisition-only programs. Learn more through the Working With Us resource.


New for 2020 is the start of our development pipeline for macromolecular microED. Potential early adopters are encouraged to contact us for more information on our plans and to discuss opportunities for sample submission and analysis. 

  • 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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Speak with our experts about using Single Particle Analysis to support your drug discovery efforts.

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