New Collaboration — Creative Biostructure × High Q Technologies

FATHOM® EPR Spectroscopy for Protein Dynamics Powered by Quantum Sensing

Creative Biostructure has partnered with High Q Technologies to deliver the world’s most advanced EPR platform for structural biology, enhanced by quantum sensing technology. Resolve protein conformations, dynamics, and interactions with greater sensitivity, higher reliability, and dramatically reduced sample volumes.

Explore EPR Services View Workflow ↓

Fast Turnaround Days Not Weeks

2–8nm Distance Range

No Limit Protein Size

Creative Biostructure

High Q Technologies

Collaboration Established March 2026 · Waterloo, Canada

The Problem

Cryo-EM, AlphaFold, and X-ray crystallography reveal what proteins look like — but biological function lives in the motion they leave unresolved: the loops that flex, the domains that switch, the conformational ensembles that decide how molecules bind.

Solution

FATHOM^® resolves that motion — measuring nanoscale distance distributions and conformational dynamics in micromolar samples, in under two hours, on a system designed for the structural biology lab.

Discover FATHOM^® →

EPR, NMR, HDX-MS & Cryo-EM

Orthogonal Approaches to
Elucidating Protein Conformation

Combining EPR, HDX-MS, Cryo-EM and NMR provides complementary insights into protein structure and dynamics that cannot be achieved using a single structural biology modality alone.

Stock et al. Nat. Commun. 9, 4971 (2018) · Adapted with NMR integration

EPR Refines Cryo-EM Structures

A low-resolution Cryo-EM structure resolved by EPR spectroscopy

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The Science

What is Electron Paramagnetic Resonance?

EPR is a biophysical characterization technique that uses paramagnetic spin labels to measure nanoscale distance distributions within and between biomolecules. Biological samples typically have no extraneous paramagnetic background signals, making EPR exceptionally specific and unambiguous.

EPR is not restricted by protein size, and captures the full ensemble of conformations — not an averaged frozen-state.

No size limitations — ideal for proteins too large for NMR or too small for Cryo-EM
Captures dynamics — measures conformational equilibria and intrinsically disordered proteins
High specificity — Low to No competing signals in biological conditions

EPR — The Biophysical Ruler

Pulsed Dipolar Spectroscopy

Primary technique

2–8 nm

Measurable range

3.5 µL

Sample volume

Low µM

Concentration

How EPR Reads Protein Dynamics

Distance Distributions Reveal Conformational States

FATHOM DEER signals encode local structural information of flexible macromolecules. Modulation frequency provides distance (1–10 nm); modulation damping characterises flexibility.

Key Applications

Dynamics & Disorder — The New Frontier

Flexible and disordered targets are the "next hurdle in drug discovery" (Nature Reviews, Lazar et al. 2025). FATHOM® EPR is uniquely positioned to address all of them.

Lazar, T. et al. Nat Rev Drug Discov 24, 743–763 (2025).

Ligand-Induced Conformational Changes & GPCRs

G-Protein Coupled Receptors are the target of over 30% of FDA-approved drugs. Precise EPR distance distributions combined with molecular modeling characterise subtle GPCR conformational changes to better understand and target their signaling behaviour.

Protein–Protein Complexes & Targeted Protein Degradation

Targeted protein degraders such as PROTACs and molecular glues form ternary complexes to destroy previously undruggable proteins in cancers and immune disorders. Intermolecular EPR constraints reveal complex formation and quaternary structural arrangements inaccessible by standard methods.

Dynamics & Intrinsically Disordered Proteins (IDPs)

IDPs such as amyloid-β and tau proteins are responsible for Alzheimer's and severe neurodegenerative diseases. While dynamic features elude NMR, Cryo-EM, and X-ray crystallography, EPR reports a probability distribution of distances inherently sensitive to flexibility and disorder.

Structural Validation for Cryo-EM & AlphaFold

AlphaFold and Cryo-EM have transformed protein structure determination. Maximise instrument time by pre-screening protein conformation with EPR. EPR distance constraints offer simple, point-to-point validation of AlphaFold predictions and Cryo-EM structural models.

The Quantum Advantage

Why High Q's FATHOM® Changes Everything

High Q Technologies applies patented quantum technology to EPR spectroscopy, using superconducting microstrip resonators to achieve unprecedented sensitivity and stability. Quantum sensing enables FATHOM® to satisfy the demanding product requirements of real-world biotechnology applications.

Quantum Sensor

Higher Sensitivity

Patented planar superconducting resonators with large filling factors and small mode volumes amplify signal detection, enabling measurements on low-concentration samples.

Quantum Device

Sample Throughput

Load a 5-sample cartridge and push start. Multi-sample handling with automated calibration and reporting removes the expert-only bottleneck, enabling high-throughput structural biology.

FATHOM® System

EPR Workflow

From Sample to Structural Insight

Our end-to-end quantum EPR service, powered by High Q's FATHOM® spectrometer and Creative Biostructure's structural biology expertise, delivers high-confidence distance data in a fraction of traditional time.

Live Performance Data

5 samples measured in 12 hrs

Automated DEER acquisition of 3.5 µL biradical samples with automated calibration included. Accurate and efficient over the full 2–8 nm range.

3.5 µL

Sample volume

Fast

Turnaround

2–8 nm

Distance range

Time domain S(t)

Distance P(r)

Protein Production & Sample Prep

Expression, purification, and quality control of target protein — including membrane proteins, complexes, and IDPs.

Site-Directed Spin Labeling

Cysteine mutagenesis at strategic positions followed by attachment of nitroxide spin labels.

PDS Measurement

Pulsed EPR distance measurements on High Q's FATHOM® quantum-enabled spectrometer.

FATHOM® Quantum EPR

Data Analysis & Distance Distribution

Integrated processing to extract probability distributions of inter-spin distances.

Structural Integration & Report

Integration with Cryo-EM, AlphaFold, or X-ray models. Full analysis report, raw data, and expert consultation.

Our Partnership

Creative Biostructure × High Q Technologies

This collaboration unites Creative Biostructure’s world-class structural biology service platform with High Q Technologies’ pioneering quantum-enabled FATHOM® EPR spectrometer. Together, we offer clients in academia and the pharmaceutical industry access to cutting-edge EPR-based molecular dynamics information, — unlocking insights into protein conformations, flexibility, and complex formation that were previously inaccessible.

High Q Technologies is headquartered in Waterloo, Canada — the heart of Canada’s Quantum Valley. Their measurement service is now integrated into Creative Biostructure’s global structural biology service network, effective March 2026.

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Structural Biology

Creative Biostructure

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High Q Technologies

Collaboration Est.

March 2026

For Research or Industrial Raw Materials, Not for Personal Use!

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