Structure Matters
We offer unparalleled expertise in solving protein structures with cutting edge cryogenic electron microscopy (cryo-EM).
Our team has a proven track record of handling the most challenging, non-crystallizable proteins, delivering high-resolution three-dimensional maps and structural data that are crucial for accelerating drug discovery.
Single Particle Analysis Resolves Details of Ligand Binding Sites and Interactions
Obtain functional insights into your macromolecules and biologics by visualizing your target’s structural components and binding sites to accelerate drug design and development.
With cryo-EM, structural biologists can easily answer questions regarding the interactions of the small molecules with the chosen target and suggest ways to help design and optimize drug candidates, supporting a structure-based drug design approach.
Overcome Obstacles in Structure Determination with Cryo-EM
Cryo-EM can overcome the challenges of traditional methods like x-ray crystallography and NMR spectroscopy, providing structural information for samples in near-native states.
XRC is popular, however crystallizing proteins can be difficult and sometimes requires extensive modifications of a protein’s native structure.
NMR spectroscopy can be done in solution on full length proteins, but its use is limited to small, highly homogenous, generally soluble biomolecules.
Cryo-EM Structure Determination is Simple with NIS
Unparalleled Structure Determination Experience
With structures solved weekly, we have extensive expertise in multiple target classes.
Target Classes Solved at NIS
- Protein Degraders & Ternary Complexes
- PROTAC® Degraders
- Molecular Glues
- Protein Degraders & Ternary Complexes
- PROTAC® Degraders
- Molecular Glues
Structures We've Solved
Frequently Asked Questions
Why choose cryo-EM over other analytical methods?
Can I see an example report for single particle analysis?
Why should I use cryo-EM instead of X-ray Crystallography or Nuclear Magnetic Resonance (NMR) spectroscopy?
Can we obtain additional/new information from cryo-EM after other methods failed?
Is cryo-EM 3 Å resolution better than crystallography 3 Å?
What kind of samples do you have experience with?
We are not sure if we can fully commit to a cryo-EM project. What are our options?
Are there size requirements?
What quantity of my sample is required?
Are all reagents and buffer conditions amenable to cryo-EM?
Do you do different concentration ranges, how does it work?
What is the wait time to start a project?
What are the turnaround times for cryo-EM structure determination projects?
Do we prepare target proteins?
How long does it take for NIS to begin imaging our samples?
What is the timeline for protein production to structure?
What documentation does NIS handle?
