EPR spectra were recorded with a Bruker EMXmicro spectrometer equipped with a ER4119HS resonator, and ER4141VT temperature control unit (Bruker Biospin, Billerica, MA). For analysis of naked radicals, the spectrophotometer was set at the following parameters unless otherwise stated: temperature, 100 K; sweep width, 300 G; modulation amplitude, 1 G; modulation frequency, 100 KHz; microwave power, 10 mW. For analysis of spin-trapped radicals (100 μM DMPO), the spectrophotometer was set at the following parameters unless otherwise stated: temperature, 298 K; sweep width, 150 G; modulation amplitude, 1 G; modulation frequency, 100 KHz; microwave power, 10 mW. Samples were equilibrated for 3 min before recording spectra.
Er4119hs resonator
Manufactured by Bruker
Sourced in United States
The ER4119HS resonator is a high-sensitivity resonator designed for use in electron paramagnetic resonance (EPR) spectrometers. The core function of this resonator is to provide a controlled electromagnetic field for the analysis of paramagnetic samples.
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Lab products found in correlation
Emx spectrometer, by Bruker (3 mentions)
Emxmicro spectrometer, by Bruker (2 mentions)
Emx spectrophotometer, by Bruker (2 mentions)
Xepr software package, by Bruker (1 mentions)
Premiumx ultra low noise microwave bridge, by Bruker (1 mentions)
Elexsys e500 spectrometer, by Bruker (1 mentions)
Elexsys e580 spectrometer, by Bruker (1 mentions)
Emxmicro, by Bruker (1 mentions)
Emxplus spectrometer, by Bruker (1 mentions)
Emx epr spectrometer, by Bruker (1 mentions)
11 protocols using er4119hs resonator
1
EPR Spectroscopy of Radical Species
2
Continuous Wave EPR Spectroscopy of Membrane Proteins
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Continuous wave (CW) EPR spectra were recorded for samples placed into Quartz capillaries (VitroComInc., New Jersey) using a Bruker EMX spectrophotometer fitted with an ER4119HS resonator. For lipid titration experiments of EHD2, and Syt1 MLVs composed of 3:1 wt/wt POPS:POPC were suspended in 20 mM Hepes, pH 7.4, 150 mM NaCl, as well as 1 mM Ca2+ in the case of synaptotagmin1, or 2:1 wt/wt POPG:POPE in the same buffer system for amphiphysin. CW EPR spectral amplitudes were recorded for samples of spin labeled protein in 20 mM Hepes, pH 7.4, 150 mM NaCl buffer. For all experiments, protein concentration was 10 μM and the amount of lipids added was varied. The values were then normalized relative to the protein’s CW EPR spectral amplitude from the protein alone in solution. For signal to noise reasons, we recorded the ratio of the amplitude of the immobilized component in the low field transition line and that of the central line width to plot the effect of increasing lipid concentrations.
3
Electron Paramagnetic Resonance of Photoactive Complex
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All electron paramagnetic resonance spectra were recorded on a Bruker EMX-micro spectrometer equipped with an EMX-Primium bridge and an ER4119HS resonator. Individual solutions were deoxygenated before mixing and the final sample concentrations were 230–250 μM protein, 20–30 μM [Ru(bpy)3]2+, and 4.5 mM [Co(NH3)5Cl]2+. Each sample was ∼100 μL and contained in a flat cell. A dark spectrum was recorded before the sample was exposed to in situ continuous illumination of a 447.5 nm LED (same setup as above) at ambient atmosphere. EPR settings: microwave frequency, 9.85 GHz; microwave power 6.3 mW; modulation frequency 100 kHz; modulation amplitude 0.1 mT. The Xepr software package (Bruker) was used for data acquisition and processing.
4
Electron Paramagnetic Resonance of Fe-TiO2
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Samples for Electron Paramagnetic Resonance (EPR) spectroscopy were prepared by loading a 4 mm EPR cell with 0.0715 g Fe–TiO2 powder containing 0.07 at% of Fe. The samples were degassed overnight on a Schlenk line under dynamic vacuum (5 × 10−3 mbar) at 393 K.
X-band, continuous wave (CW) EPR analysis was performed with a Bruker EMX spectrometer equipped with a ER4119HS resonator operating at 120 K under a liquid nitrogen-cooled nitrogen flow. Spectra were recorded using the following instrumental conditions: 1 × 104 receiver gain; 100 kHz magnetic field modulation frequency; 5.0 Gauss magnetic field modulation amplitude and 20.2 kHz microwave power.
Irradiation was performed ex situ at 77 K in a Dewar filled with liquid nitrogen, using a Labino Nova 365 nm (350 to 395 nm bandwidth) UV-A LED light source (213 mW typical output).
Experimental spectra were simulated using the EasySpin package33 (link) operating within the Mathworks Matlab environment.
X-band, continuous wave (CW) EPR analysis was performed with a Bruker EMX spectrometer equipped with a ER4119HS resonator operating at 120 K under a liquid nitrogen-cooled nitrogen flow. Spectra were recorded using the following instrumental conditions: 1 × 104 receiver gain; 100 kHz magnetic field modulation frequency; 5.0 Gauss magnetic field modulation amplitude and 20.2 kHz microwave power.
Irradiation was performed ex situ at 77 K in a Dewar filled with liquid nitrogen, using a Labino Nova 365 nm (350 to 395 nm bandwidth) UV-A LED light source (213 mW typical output).
Experimental spectra were simulated using the EasySpin package33 (link) operating within the Mathworks Matlab environment.
5
Spin-Labeled GlpG Reconstitution in E.coli Liposomes
6
Continuous Wave EPR and ENDOR Spectroscopy
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The continuous wave (CW) X-band EPR measurements were performed on a Bruker EMX spectrometer utilizing an ER4119HS resonator, 100 kHz field modulation at 140 or 298 K, and typically using 10.17 mW MW power. The CW Q-band EPR and ENDOR measurements were recorded on a Bruker Elexsys E500 spectrometer using a Bruker ER5106 QT-E Qband resonator operating at 10 kHz field modulation and 10 K for ENDOR (and at 100 kHz and 50 K for the EPR). The CW ENDOR spectra were obtained using 5 dB RF attenuation (80 W) from an ENI 3200L RF amplifier at 100 kHz RF modulation depth and 0.5 mW microwave power. Additional X-band Davies ENDOR measurements were also obtained. These Daviesâ€"ENDOR experiments (10) were recorded on a Bruker Elexsys E580 spectrometer and carried out using the following pulse sequence: Ï€-T-Ï€/2-Ï"-Ï€-Ï"-echo. The experiments were done with mw pulse lengths of t Ï€ = 256 ns, t Ï€/2 = 128 ns, and an interpulse time Ï" of 800 ns. An rf Ï" pulse of variable frequency and a length of 18 μs were applied during time T of 20 μs.
7
Annexin-Membrane Interaction Characterization
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For EPR measurements, annexin protein (ANXB12 or ANXA2) were mixed with 600 μg of the extruded vesicles (POPS/POPC molar ratio 2 to 1) in 20 mM HEPES, 100 mM NaCl, pH 7.4 with 1 mM CaCl2 (protein-to-lipid molar ratio ~1:450) in a total volume of 1000 ul. The lipid vesicles as well as the membrane-bound annexins were harvested by centrifugation (21,000 × g, room temperature, 20 minutes). After carefully removing the supernatant, the pellet was collected into a borosilicate glass capillary to record EPR spectra using a Bruker EMX spectrophotometer fitted with ER4119HS resonator (scan width 150 G, modulation amplitude 1.5 G). All spectra were normalized to the same number of spins using double integration. The central line amplitudes from the normalized spectra were converted to fold increase over the 100% labelled ANXB12-K132C mutant and plotted. Estimates of trimer formation were then obtained from the spectral amplitudes of the respective normalized spectra assuming a linear combination of the individual spectral components of Fig. 3e .
8
Harwell Alanine Dosimeter Characterization
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The Harwell alanine dosimeter consisted of 90.9% L-alpha-alanine and 9.1% paraffin wax as a binder. These dosimeters were 4.8 ± 0.1 mm in diameter and 2.8 ± 0.1 mm in height, and mass was 60.0 ± 2.0 mg within the overall batch and ± 0.6 mg within a lot (standard deviation of 0.3 mg). This study used alanine batch number BY616. The electron paramagnetic resonance (EPR) spectroscopy (Bruker EMXmicro) is an X-Band machine installed with a standard ER 4119HS resonator (Bruker BioSpin Corporation). The EPR operation parameter was optimized at the radiotherapy level of 1–20 Gy. The acquisition parameters were set as follows: microwave power (MP): 2 mW, modulation amplitude (MA): 7.018 G, time constant (TC): 40.96 ms, center field: 3500 G, sweep width: 200 G, modulation frequency: 100 kHz, sweep time: 40.45 s, receiver gain: 30 dB, and number of scans: 3 times.
9
Spin-Labeling of Oxidized Tau Monomers
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CW EPR spectroscopy was used to confirm that the cysteines in htau40 Ox monomers were inaccessible for thiol crosslinking. For this purpose, purified protein was taken up in 8 M GdnHCl and incubated for 1 h at 22 °C with a 10-fold molar excess of the paramagnetic spin label MTSL (Toronto Research Chemicals taken up in dimethyl sulfoxide to 40 mg/ml). Excess label and denaturant were removed by gel filtration using PD-10 columns. The labeling procedure was repeated with nonoxidized htau40 monomers and oxidized monomers (htau40 Ox) that had been incubated with 20 mM DTT for 5 h (to reduce the disulfide bonds) and then dialyzed (to remove DTT). Both samples were expected to have free cysteines available for labeling and thus served as controls. CW EPR spectra (20 scans) of samples containing 5 μM monomers were collected at X-band (9.5 GHz) at 22 °C with 150 G sweep width, 12.05 mW power, and 1 G modulation amplitude on a Bruker EMX Plus spectrometer fitted with an ER 4119HS resonator.
10
Quantitative EPR Spectroscopy of Copper
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