Structural Biology

NIS Molecule

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.

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In House Cryo-EM Infrastructure

With 6 microscopes on 2 coasts, we provide high quality data & seamless project execution, no matter where you are.

Our Platform
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Unprecedented Speed

Our advanced cryo-EM workflows deliver 3D protein structures in as little as 2 weeks, revolutionizing your research timelines.

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Unmatched
Expertise

With 240+ cumulative years of cryo-EM experience, we are the most experienced structural biology CRO.

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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.

Learn how cryo-EM compares to XRC & NMR.

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Cryo-EM Structure Determination is Simple with NIS

With personalized cryo-EM workflows, projects with NIS are simple and streamlined.

Unparalleled  Structure Determination Experience

With structures solved weekly, we have extensive expertise in multiple target classes.

Structures We've Solved

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The Cryo-EM structure of human serum albumin in complex with ligands

September 1, 2024
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Mechanistic insights into a heterobifunctional degrader-induced PTPN2/N1 complex

August 16, 2024
Read the latest research collaboration between Calico Life Sciences, AbbVie, C4 Therapeutics, and NIS, solving phosphatase structures supported by cryo-EM data collection.
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High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy

April 20, 2024
Structural analysis of membrane proteins is often challenging due to low protein yields and their unstable nature. HiTehA is particularly challenging due to its encapsulation in detergent micelles, which obstructs proper alignment of projections needed for 3D structure reconstruction.
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Structural basis for the oligomerization-facilitated NLRP3 activation

February 7, 2024
Using cryo-EM structures, researchers propose an activation mechanism for NLRP3.
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Integrative structural and functional analysis of human malic enzyme 3: A potential therapeutic target for pancreatic cancer

December 18, 2022
Janssen Research used an integrative structural biology approach to study human malic enzyme 3 (ME3), a potential therapeutic target for pancreatic cancer.
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Cryo-EM structures of inhibitory antibodies complexed with arginase 1 provide insight into mechanism of action

July 29, 2021
Merck Used cryo-EM to Gain Insight Into Mechanism of Action by Imaging Structures of Inhibitory Antibodies Complexed with Arginase 1.
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Frequently Asked Questions

Why choose cryo-EM over other analytical methods?

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Can I see an example report for single particle analysis?

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Why should I use cryo-EM instead of X-ray Crystallography or Nuclear Magnetic Resonance (NMR) spectroscopy?

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Can we obtain additional/new information from cryo-EM after other methods failed?

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Is cryo-EM 3 Å resolution better than crystallography 3 Å?

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What kind of samples do you have experience with?

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We are not sure if we can fully commit to a cryo-EM project. What are our options?

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Are there size requirements?

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What quantity of my sample is required?

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Are all reagents and buffer conditions amenable to cryo-EM?

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Do you do different concentration ranges, how does it work?

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What is the wait time to start a project?

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What are the turnaround times for cryo-EM structure determination projects?

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Do we prepare target proteins?

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How long does it take for NIS to begin imaging our samples?

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What is the timeline for protein production to structure?

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What documentation does NIS handle?

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