Journal
SCIENCE ADVANCES
Volume 5, Issue 10, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aay1394
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Funding
- European Union Horizon 2020 Marie Sklodowska-Curie Fellowship [745702]
- Max Planck Society
- Sonderforschungsbereich by Humboldt Universitat zu Berlin [Sfb1078]
- Cluster of Excellence-2033 RESOLV (Deutsche Forschungsgemeinschaft, DFG) [390677874]
- DFG Research Training Group Microbial Substrate Conversion (MiCon) [GRK 2341]
- Volkswagen Stiftung (Design of [FeS] cluster containing MetalloDNAzymes) [Az 93412]
- Marie Curie Actions (MSCA) [745702] Funding Source: Marie Curie Actions (MSCA)
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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 micro-helix 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 (Clostridium pasteurianum; Cpl) with dimensions of 0.3 mm by 0.1 mm by 0.1 mm, yielding a proposed g-tensor orientation of the H-ox state.
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