ArticleScience advances2019
Extending electron paramagnetic resonance to nanoliter volume protein single crystals using a self-resonant microhelix.
Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- EPR spectroscopy 80 years after its discovery.Science advances · 2026Review
- Continuous-flow electron spin resonance microfluidics device with sub-nanoliter sample volume.Journal of magnetic resonance open · 2025Article
- Microwave field mapping for EPR-on-a-chip experiments.Science advances · 2024Article
- Recent advances in microresonators and supporting instrumentation for electron paramagnetic resonance spectroscopy.The Review of scientific instruments · 2022Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Scalable microresonators for room-temperature detection of electron spin resonance from dilute, sub-nanoliter volume solids.Science advances · 2020Article
- Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Distance measurement between trityl radicals by pulse dressed electron paramagnetic resonance with phase modulation.Magnetic resonance (Gottingen, Germany) · 2020Article
- Hyperfine spectroscopy in a quantum-limited spectrometer.Magnetic resonance (Gottingen, Germany) · 2020Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electron paramagnetic resonance (EPR) spectroscopy on protein single crystals is the ultimate method for determining the electronic structure of paramagnetic intermediates at the active site of an enzyme and relating the magnetic tensor to a molecular structure. However, crystals of dimensions typical for protein crystallography (0.05 to 0.3mm) provide insufficient signal intensity. In this work, we present a microwave self-resonant microhelix for nanoliter samples that can be implemented in a commercial X-band (9.5 GHz) EPR spectrometer. The self-resonant microhelix provides a measured signal-to-noise improvement up to a factor of 28 with respect to commercial EPR resonators. This work opens up the possibility to use advanced EPR techniques for studying protein single crystals of dimensions typical for x-ray crystallography. The technique is demonstrated by EPR experiments on single crystal [FeFe]-hydrogenase (
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Registered trials
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