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Er 4102 st resonator

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The ER 4102 ST resonator is a versatile laboratory equipment designed to generate and manipulate electromagnetic fields. It serves as a core component in various scientific and research applications that require the use of electron spin resonance (ESR) or electron paramagnetic resonance (EPR) techniques. The resonator provides a controlled and stable environment for sample analysis, allowing researchers to study the properties and behaviors of materials at the atomic and molecular levels.

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Lab products found in correlation

Esp 300 spectrometer, by Bruker (4 mentions) Elexsys e540 x band spectrometer, by Bruker (2 mentions) Er 4112 hv helium flow cryostat, by Bruker (2 mentions) Itc 502, by Oxford Instruments (2 mentions) Elexsys e680 epr spectrometer, by Bruker (1 mentions) Easyspin toolbox, by MathWorks (1 mentions) Continuous flow helium cryostat, by Oxford Instruments (1 mentions) Esr900, by Oxford Instruments (1 mentions) Emx spectrometer, by Bruker (1 mentions)

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ER 4102

8 protocols using er 4102 st resonator

1

EPR Spectroscopy of Low-Temperature Samples

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The CW EPR spectra were measured on an ELEXSYS E540 X-band spectrometer (Bruker-Biospin, Billerica, MA) with an ER 4102 ST resonator using 100 kHz magnetic field modulation. Spectra were measured at 77 K in a liquid-nitrogen quartz insertion dewar and at lower temperatures with a Bruker ER 4112 HV helium flow cryostat. Care was taken to avoid microwave power saturation or modulation broadening in the CW EPR spectra that are reported or analyzed.
Krzyaniak M.D., Cruce A.A., Vennam P., Lockart M., Berka V., Tsai A.L, & Bowman M.K. (2016). The tetrahydrobiopterin radical with high- and low-spin heme in neuronal nitric oxide synthase -- a new indicator of the extent of NOS coupling. Free radical biology & medicine, 101, 367-377.
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2

Continuous-Wave and HYSCORE EPR Spectroscopy

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CW EPR spectra were measured on a Bruker ELEXYS E540 X-band spectrometer with an ER 4102 ST resonator (Bruker-Biospin, Billerica, MA). CW spectra were measured at a nominal microwave frequency of 9.45 GHz. Spectra were recorded at 77 K using a liquid-nitrogen quartz insertion Dewar or at 15 K using a Bruker ER 4112 HV helium flow cryostat.
HYSCORE measurements were made at 10–15 K with a nominal microwave frequency of 9.76 GHz using an ELEXSYS E680 EPR spectrometer (Bruker-Biospin, Billerica, MA) equipped with a Bruker Flexline ER 4118 CF cryostat and an ER 4118X-MD4 ENDOR resonator. HYSCORE measurements used a four pulse sequence, π/2−τ−π/2−t1−π−t2−π/2−τ−echo repeated at a rate of 2 kHz, where π/2 and π represent pulses 16 and 32 ns long, respectively, and t1, t2, and τ are delays between the pulses. The times t1 and t2 are varied independently to create the two dimensions of the HYSCORE spectrum. The delay time τ was set to 240 ns for all measurements except CYP2C9d with no drug added at 296.5 mT, which had a τ value of 288 ns to give a slightly more intense signal.
Lockart M.M., Rodriguez C.A., Atkins W.M, & Bowman M.K. (2018). CW EPR Parameters Reveal Cytochrome P450 Ligand Binding Modes. Journal of inorganic biochemistry, 183, 157-164.
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3

EPR Analysis of Persimmon Extract Effects

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A Bruker ESP 300 spectrometer (Bruker, Rheinstetten, Germany) equipped with an ER 4102 ST resonator was used to perform the EPR measurements. The instrument parameters were as follows: microwave power, 2 mW; modulation frequency, 100 kHz; modulation amplitude, 1.0 G; magnetic field scan, 100 G; sweep time, 168 s; and detector time constant, 41 ms; receive gain, 105. All measurements were performed at room temperature (24–26 °C). Hydroxyl radicals formed by Fenton reagents (50 µM Fe(II) and 100 µM H2O2) in buffered media (10 mM phosphate, pH 7.2) were trapped by DMPO (20 mM) (Zalomaeva et al., 2007 (link)). The effect of different concentrations of persimmon extract was investigated against DMPO hydroxylation. Spectra were acquired until 3 min after reaction started and the quantification of DMPO-OH adduct was done by measurement of first line resonance peak height diminished of EPR baseline signal.
Dalvi L.T., Moreira D.C., Alonso A., de Avellar I.G, & Hermes-Lima M. (2018). Antioxidant activity and mechanism of commercial Rama Forte persimmon fruits (Diospyros kaki). PeerJ, 6, e5223.
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4

Biomimetic Membrane Conformational Analysis

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The biomimetic membranes were impregnated, as described above. Spin labeling technique was employed to examine the conformational structure of the membrane using 5-DSA or 16-DSA. EPR was performed using a Bruker ESP 300 spectrometer (Bruker, Rheinstetten, Germany) equipped with an ER 4102 ST resonator. The instrument settings were microwave power of 2 mW; modulation frequency of 100 KHz; modulation amplitude of 1.0 G; magnetic field scan of 100 G; sweep time of 168 s; and a detector time constant of 41 ms. EPR spectral simulations were performed using the nonlinear-least-squares (NLLS) program for an isotropic model. The biomimetic membrane was introduced into flat, quartz EPR cell to perform the EPR measurements at room temperature (~25°C).
de Souza Teixeira L., Vila Chagas T., Alonso A., Gonzalez-Alvarez I., Bermejo M., Polli J, & Rezende K.R. (2020). Biomimetic Artificial Membrane Permeability Assay over Franz Cell Apparatus Using BCS Model Drugs. Pharmaceutics, 12(10), 988.
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5

EPR Spectroscopy at X-Band

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EPR spectra at X-Band (~9.5 GHz) were acquired on a Bruker ESP-300 spectrometer equipped with an ER/4102 ST resonator (Bruker), an Oxford Instruments continuous-helium-flow cryostat, and an Oxford Instruments temperature controller (ITC 502). For all experiments, quartz tubes with 3 mm inner and 4 mm outer diameters were used (QSI).
Rajakovich L.J., Pandelia M.E., Mitchell A.J., Chang W.C., Zhang B., Boal A.K., Krebs C, & Bollinger JM J.r. (2019). A new microbial pathway for organophosphonate degradation catalyzed by two previously misannotated non-heme-iron oxygenases. Biochemistry, 58(12), 1627-1647.
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6

CW EPR Measurements and Simulations

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CW EPR measurements were made on a Bruker ELEXSYS E540 X-band spectrometer with an ER 4102 ST resonator and a quartz liquid nitrogen insertion dewar. Spectra were recorded at 77 K with a nominal microwave frequency of 9.45 GHz, a modulation amplitude and frequency of 5.0 G or 10.0 G and 100 kHz, respectively, and a microwave power of 3.34 mW or 6.64 mW. CW EPR simulations were made using the EasySpin toolbox in MATLAB (Mathworks, R2018a) [17 (link)]. Simulations included g-values, g-strains, and weights for each component in the EPR spectrum. The g-value in EPR describes the peak position with respect to the microwave frequency and magnetic field, the g-strains are related to line widths and account for Gaussian distributions of the g-values, and the weights describe each spectral component’s relative contribution to the overall spectrum [17 (link)]. With the exception of the drug-free spectrum, each spectrum is the sum of several overlapping spectra. In these cases, the overall spectrum was simulated with one component using the drug-free parameters first, and additional components were added as necessary to match the experimental spectrum. In some cases, it appears that some drug-free enzyme remained after drug binding; these components have the same g-values as the drug-free spectrum and are identified as “resting state” in binding assignments.
Lockart M.M., Butler J.T., Mize C.J., Fair M.N., Cruce A.A., Conner K.P., Atkins W.M, & Bowman M.K. (2020). Multiple Drug Binding Modes in Mycobacterium tuberculosis CYP51B1. Journal of inorganic biochemistry, 205, 110994.
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7

CW EPR Spectroscopy of RFQ Samples

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CW X-band EPR spectra of RFQ samples were collected at 10 K at Pennsylvania State University using a Bruker ESP-300 spectrometer (~9.5 GHz) equipped with an ER/4102 ST resonator (Bruker), a continuous flow helium cryostat (Oxford Instruments), and a temperature controller (ITC 502, Oxford Instruments).23 (link) All other CW X-band EPR spectra from 5–30 K (9.62 GHz) were collected at the Ohio Advanced EPR Facility at Miami University using a Bruker EMX instrument equipped with an Oxford Instruments continuous flow helium cryostat and temperature controller (ESR 900). For time-dependent studies of product formation, the temperature was set to 6.67 K to avoid saturation artifacts.17 (link) Spectra were obtained using a microwave power of 20 mW and a modulation frequency and amplitude of 100 kHz and 10 G, respectively. Spin quantitation was carried out using a 250 μM copper(II) azurin standard measured under non-saturating conditions (200 μW).
Miller E.K., Trivelas N.E., Maugeri P.T., Blaesi E.J, & Shafaat H.S. (2017). Time-Resolved Investigations of Heterobimetallic Cofactor Assembly in R2lox Reveal Distinct Mn/Fe Intermediates. Biochemistry, 56(26), 3369-3379.
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8

EPR Spectra Analysis of Aqueous Protein Samples

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Room temperature EPR spectra were measured using an X-band Bruker EMX spectrometer fitted with the ER4102ST resonator used in combination with the 19-bore AquaX cell for measurements on aqueous samples. The following conditions were used: microwave power of 2 mW; modulation frequency of 100 kHz; modulation amplitude of 1.0 G. attached at the same sites are both broader compared to R1 spectra corresponding to a slower motional regime although the label Rn at 58C site is clearly the less mobile. Also noticeable, at site S117 the spectrum of Rn is distinctly broader compared to the one of R1 indicating lower degree of the label sidechain mobility.
Oganesyan V.S., Chami F., White G.F, & Thomson A.J. (2017). A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics. Journal of magnetic resonance (San Diego, Calif. : 1997), 274.
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