Shqe resonator

Manufactured by Bruker

The SHQE resonator is a high-quality resonant structure designed for use in Bruker's analytical instruments. It is a core component that enables precise electromagnetic field generation and signal detection, which are fundamental to the instrument's core functionality. The SHQE resonator is engineered to provide stable and reliable performance, supporting the accurate measurements and analyses expected from Bruker's laboratory equipment.

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Lab products found in correlation

Emx spectrometer, by Bruker (1 mentions) Liquid helium flow cryostat, by Oxford Instruments (1 mentions) Er 4112 hv, by Oxford Instruments (1 mentions) Xepr software, by Bruker (1 mentions) Elexsys e580 spectrometer, by Bruker (1 mentions) E580 spectrometer, by Bruker (1 mentions)

4 protocols using shqe resonator

CW-EPR and DEER Spectroscopy Protocol

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X-band continuous wave (CW)-EPR measurements were performed on a Bruker ESC106 spectrometer at 9.5 GHz/0.34 T with a Bruker SHQE resonator. Low-spin EPR spectra were obtained with a modulation frequency of 100 kHz at 50 K, 0.2 mW, and high-spin EPR signals were collected at 15 K, 2 mW. DEER spectra were collected on a Bruker ELEXSYS E580 spectrometer at 34 GHz using a Q-Band EN 5107D2 resonator at 20 K. The four pulsed DEER sequence was

π / 2 (ν_{probe}) \to τ_{1} \to π (ν_{probe}) \to (τ_{1} + T) \to π (ν_{pump}) \to (τ_{2} - T) \to π (ν_{probe}) \to τ_{2} \to echo

The π/2 and π pulse lengths were 16 and 32 ns for the probe pulses, respectively, 24 ns was used for the pump pulse, and the frequency difference between probe and pump pulses was 80 MHz. DEER time traces and resultant distance distributions were analyzed by DeerAnalysis 2015.³¹

Chuo S.W., Wang L.P., Britt R.D, & Goodin D.B. (2019). An Intermediate Conformational State of Cytochrome P450cam-CN in Complex with Putidaredoxin. Biochemistry, 58(18), 2353-2361.

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EPR Spectroscopy of Cu(II) Complex

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The continuous-wave (CW) EPR spectrum at 9.2 GHz, reported previously, was recorded on a Bruker EMX spectrometer in an SHQE resonator at 120 K in a frozen glass of ≈ 3 mM Tp^tBuCu^II(OCH₂CF₃) in toluene.²¹ The field axis was corrected for a 0.5 mT difference between nominal and teslameter-determined field values.
For pulse field-swept 34 GHz EPR spectroscopy, a 1.5 mM solution of Tp^tBuCu^II(OCH₂CF₃) in 1:1 DCM:toluene was flash frozen in a 1 mm O.D. quartz EPR sample tube. Pulse field-swept and Davies ENDOR spectra were recorded in the same spectrometer and resonator as described above at 10 K. The field swept spectrum was Hahn echo detected (π/2 – τ – π – τ – echo). Davies ENDOR was echo detected (π – T – π/2 – τ – π – τ – echo) with pulse lengths and timings given in the figure captions. Microwave frequencies were measured with the built-in frequency counter. Magnetic field values were corrected for a 1.5 mT shift between nominal and teslameter-determined field values.

Hayes E.C., Porter T.R., Barrows C.J., Kaminsky W., Mayer J.M, & Stoll S. (2016). Electronic Structure of a CuII-Alkoxide Complex Modeling Intermediates in Copper-Catalyzed Alcohol Oxidations. Journal of the American Chemical Society, 138(12), 4132-4145.

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Pulsed Q-band EPR Spectroscopy

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Continuous wave (CW) and pulse EPR spectra were acquired on a Bruker Elexsys E580 spectrometer equipped with a SuperX-FT microwave bridge. CW spectra were acquired at X-band frequencies using a Bruker SHQE resonator. A temperature of 7 K was maintained with an ER 4112-HV Oxford Instruments liquid helium flow cryostat.
Field-swept pulse EPR and HYSCORE spectra were acquired at Q-band frequencies by using a home-built intermediate-frequency extension of the SuperX-FT X-band bridge that has a Millitech 5W pulse power amplifier. All experiments were conducted on a home-built TE₀₁₁ resonator utilizing the open resonator concept developed by Annino et al.⁴⁸ and mechanical construction of the probehead similar to that presented by Reijerse et al.^{49 (link)} This setup allows t(π/2) = 12–16 ns at maximum input power with spectrometer dead time (including the resonator ring time) of 100–120 ns. Data acquisition and control of experimental parameters were performed by using Bruker XEPR software.

Martinie R.J., Livada J., Chang W.C., Green M.T., Krebs C., Bollinger JM J.r, & Silakov A. (2015). Experimental Correlation of Substrate Position with Reaction Outcome in the Aliphatic Halogenase, SyrB2. Journal of the American Chemical Society, 137(21), 6912-6919.

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EPR Analysis of Iron-Sulfur Clusters

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Reduction of the iron-sulfur clusters was achieved by addition of excess (5 mM) dithionite to 600 μM TvgB in storage buffer. Samples were transferred into 4 mm OD quartz tubes in the inert atmosphere chamber and flash frozen in liquid nitrogen. Tubes were temporarily capped with clamped tygon tubing, removed from the chamber, partially evacuated, back-filled with a partial pressure of helium (100 mTorr) to facilitate thermal equilibration, and flame-sealed. Samples were kept frozen in liquid nitrogen for a few hours, until they were inserted into a precooled resonator. Continuous wave EPR spectra at 20 K were acquired at 9.3683 GHz on a Bruker E580 spectrometer with an SHQE resonator and equipped with a Bruker/ColdEdge Stinger cryogenic system. Spectra were acquired with 4 G modulation amplitude at 100 kHz, 2000 G scan width, a time constant of 81 ms, sweep time of 84 s with a 7 s delay to allow field settling at the end of each scan, and signal averaging of four scans. The microwave power was selected to be in a range where the signal increases linearly with square root of power. Simulations were performed using the Bruker BioSpin software Aniso-spin fit. The g values for two overlapping signals were adjusted manually using values reported for MftC (24 (link)) as the starting points.

Kostenko A., Lien Y., Mendauletova A., Ngendahimana T., Novitskiy I.M., Eaton S.S, & Latham J.A. (2022). Identification of a poly-cyclopropylglycine–containing peptide via bioinformatic mapping of radical S-adenosylmethionine enzymes. The Journal of Biological Chemistry, 298(5), 101881.

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