Elexsys e500 spectrometer

Manufactured by Bruker

Sourced in United States, United Kingdom, Germany

The Elexsys E500 is a compact, high-performance electron paramagnetic resonance (EPR) spectrometer designed for a wide range of applications. It features a stable and sensitive detection system, allowing for the analysis of various paramagnetic species. The Elexsys E500 is capable of continuous-wave (CW) and pulsed EPR measurements, providing users with a versatile tool for their research and analysis needs.

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Lab products found in correlation

87 protocols using elexsys e500 spectrometer

Spin-labeled MamM CTD Characterization by EPR

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For metal-bound samples, freshly spin-labeled C267S MamM CTD in buffer A at ∼70 µm was used. Stock solutions of metal salts (ZnSO₄.5H₂O and CuCl₂.2H₂O) were prepared in H₂O to a final concentration of 100 mm. Aliquots (15 µl) of spin-labeled protein were incubated with a 3-fold excess of each metal salt for 40 min on ice. Aliquots of ∼10 µl were transferred to 0.8-mm (outer diameter) capillary tubes for measurement.
The ambient temperature setup for X-band cw-EPR consisted of a Bruker E500 eleXsys spectrometer fitted with an ER 4123D (dielectric RT cw-EPR) resonator. The following measuring parameters were used for data acquisition: a microwave frequency of 9.758 GHz, a modulation frequency of 100 KHz, a modulation amplitude of 1 gauss, and a microwave power of 0.2 milliwatt.

Barber-Zucker S., Hall J., Froes A., Kolusheva S., MacMillan F, & Zarivach R. (2021). The cation diffusion facilitator protein MamM's cytoplasmic domain exhibits metal-type dependent binding modes and discriminates against Mn2+. The Journal of Biological Chemistry, 295(49), 16614-16629.

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X-band cw-EPR Spectroscopy Measurements

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X-band cw-EPR measurements were performed on a Bruker E500 ELEXSYS
spectrometer equipped with the Bruker dual-mode cavity (ER4116DM)
and an Oxford Instruments helium flow cryostat (ESR 900). The microwave
bridge was the high-sensitivity bridge Super-X from Bruker (ER-049X)
with integrated microwave frequency counter. The magnetic field controller
(ER032T) was externally calibrated with a Bruker NMR field probe (ER035M).
Spectral analysis and simulations were handled by using the EasySpin
program.^{34 (link)}

Lin Y.H., Cramer H.H., van Gastel M., Tsai Y.H., Chu C.Y., Kuo T.S., Lee I.R., Ye S., Bill E, & Lee W.Z. (2019). Mononuclear Manganese(III) Superoxo Complexes: Synthesis, Characterization, and Reactivity. Inorganic Chemistry, 58(15), 9756-9765.

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Continuous-wave EPR Spectroscopy Methodology

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Continuous-wave (cw) X-band EPR measurements
were performed on a Bruker E500 ELEXSYS spectrometer equipped with
the Bruker dual-mode cavity (ER4116DM) or a standard cavity (ER4102ST)
and an Oxford Instruments helium flow cryostat (ESR 900). The microwave
bridge was a high-sensitivity Super-X bridge (Bruker ER-049X) with
integrated microwave frequency counter. The magnetic field controller
(ER032T) was calibrated with a Bruker NMR field probe (ER035M). EPR
simulations have been done with our own routines, esim_gfit and esim_sx.
For spin quantitation, the experimental derivative spectra were numerically
integrated by using the routine eview, and the results were corrected
for their g value dependence for field-swept spectra
by using Aasa and Vänngård approximation,^{32 (link)} i.e. dividing the integrals by the factor,

Chang H.C., Mondal B., Fang H., Neese F., Bill E, & Ye S. (2019). Electron Paramagnetic Resonance Signature of Tetragonal Low Spin Iron(V)-Nitrido and -Oxo Complexes Derived from the Electronic Structure Analysis of Heme and Non-Heme Archetypes. Journal of the American Chemical Society, 141(6), 2421-2434.

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Spin-Labeling of MamM-CTD Protein

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For metal-bound samples, freshly spin labelled C267S MamM-CTD, in buffer A at ~70 μM was used. Stock solutions of metal salts (ZnSO4.5H2O and CuCl2.2H2O) were prepared in H2O
to a final concentration of 100 mM. Aliquots (15 μL) of spin labelled protein were incubated with a 3-fold excess of each metal salt for 40 minutes on ice. Aliquots of ~10 μL were transferred to 0.8mm (o.d.) capillary tubes for measurement.
The ambient temperature set-up for X-band cw-EPR consisted of a Bruker E500 eleXsys spectrometer fitted with an ER 4123D (dielectric RT cw-EPR) resonator. The following measuring parameters were used for data acquisition: a microwave frequency of 9.758 GHz, a modulation frequency of 100 KHz, a modulation amplitude of 1 G, and a microwave power of 0.2 mW.

Barber-Zucker S., Hall J., Froes A.V.T.D.V., Kolusheva S., MacMillan F., & Zarivach R. (2020). The cation diffusion facilitator protein MamM’s cytoplasmic domain exhibits metal-type dependent binding modes and discriminates against Mn²⁺.

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CW-EPR Spectroscopy of Spin-Labeled Proteins

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CW-EPR spectra were recorded using an E500 Elexsys Bruker spectrometer operating at 9.0−9.5 GHz equipped with a super-high-sensitivity CW resonator. The spectra were recorded at room temperature (292 ± 5 K), at a microwave power of 20.0 mW, a modulation amplitude of 1.0 G, a time constant of 60 ms, and a receiver gain of 60.0 dB. The samples were measured in 1.0 mm quartz tubes (Wilmad-LabGlass, Vineland, NJ, USA). CW-EPR simulations were carried out using MATLAB, with the EasySpin toolbox [60 (link)]. The final spin-labeled protein concentration was between 0.01 and 0.03 mM.

Pavlin M., Qasem Z., Sameach H., Gevorkyan-Airapetov L., Ritacco I., Ruthstein S, & Magistrato A. (2019). Unraveling the Impact of Cysteine-to-Serine Mutations on the Structural and Functional Properties of Cu(I)-Binding Proteins. International Journal of Molecular Sciences, 20(14), 3462.

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CW-EPR Spectroscopy for Protein Characterization

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CW-EPR spectra were recorded using an E500 Elexsys Bruker spectrometer operating at 9.0−9.5 GHz and equipped with a super-high-sensitivity CW resonator. The spectra were recorded at room temperature (292 ± 5 K), at a microwave power of 20.0 mW, a modulation amplitude of 1.0 G, a time constant of 60 ms, and a receiver gain of 60.0 dB. The samples were measured in 1.0-mm quartz tubes (Wilmad-LabGlass, Vineland, NJ, USA). The final spin-labeled protein concentration was between 0.01 and 0.03 mM.

Zaccak M., Qasem Z., Gevorkyan-Airapetov L, & Ruthstein S. (2020). An EPR Study on the Interaction between the Cu(I) Metal Binding Domains of ATP7B and the Atox1 Metallochaperone. International Journal of Molecular Sciences, 21(15), 5536.

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Continuous Wave EPR Spectroscopy

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CW‐EPR (Continuous wave EPR) spectra were recorded using E500 Elexsys Bruker spectrometer operating at 9.0–9.5GHz. The spectra were recorded at room temperature at microwave power of 20.0 mW, modulation amplitude of 1.0 G, a time constant of 60 ms, and receiver gain of 60.0 dB. The samples were measured in 0.8 mm capillary quartz tubes (Vitrocom).

Yakobov I., Mandato A., Hofmann L., Singewald K., Shenberger Y., Gevorkyan‐Airapetov L., Saxena S, & Ruthstein S. (2022). Allostery‐driven changes in dynamics regulate the activation of bacterial copper transcription factor. Protein Science : A Publication of the Protein Society, 31(5), e4309.

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CW-EPR Spectroscopy Protocol for Biomolecules

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CW-EPR spectra were recorded using
an E500 Elexsys Bruker spectrometer operating at 9.0–9.5 GHz
equipped with a super-high-sensitivity CW resonator. The spectra were
recorded at low temperature (130 ± 5 K) at a microwave power
of 20.0 mW, a modulation amplitude of 1.0 G, a time constant of 80
ms, and a receiver gain of 60.0 dB. The samples were measured in 4.0
mm quartz tubes (Wilmad-LabGlass, Vineland, NJ). CW-EPR simulations
were carried out using MATLAB with the EasySpin toolbox.^{33 (link)}

Walke G.R, & Ruthstein S. (2019). Does the ATSM-Cu(II) Biomarker Integrate into the Human Cellular Copper Cycle?. ACS Omega, 4(7), 12278-12285.

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Low-Temperature CW-EPR Spectroscopy of Cu(II)

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Cu(II) low-temperature continuous wave (CW)-EPR measurements were performed using an E500 Elexsys Bruker spectrometer operating at 9.0–9.5 GHz, equipped with a high-sensitivity CW resonator. Spectra were recorded at low temperature (130 ± 5 K) at a microwave power of 20.0 mW, modulation amplitude of 4.0 G, a time constant of 120 ms, and receiver gain of 60.0 dB. The samples were measured in a 1.0-mm quartz tube (Wilmad-LabGlass, Vineland, NJ) placed in a 4.0-mm quartz tube for cooling. CW-EPR simulations were carried out using MATLAB, with the EasySpin toolbox (23 (link)).

Walke G., Aupič J., Kashoua H., Janoš P., Meron S., Shenberger Y., Qasem Z., Gevorkyan-Airapetov L., Magistrato A, & Ruthstein S. (2022). Dynamical interplay between the human high-affinity copper transporter hCtr1 and its cognate metal ion. Biophysical Journal, 121(7), 1194-1204.

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Quantifying Spin Labeling Efficiency

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To determine the labeling efficiency of His-MxiC(Cys) with MTSL, continuous wave EPR spectra were detected at room temperature on an E500 Elexsys Bruker spectrometer equipped with a super high Q cavity. The samples were thawed on ice, and 20 μl were transferred into a 1.5-mm outer diameter glass capillary. A 14-mT field sweep was performed, with 0.15 mT modulation amplitude, 7.96 milliwatt incident microwave power, and ∼9.38 GHz frequency. As the measured signal is the first derivative, the resulting curve has to be integrated to obtain the absorbance spectrum. Double integration yields the spin concentration as horizontal asymptote. The area under the absorbance spectrum is proportional to the spin concentration. The correlation factor was experimentally determined with a solution of known concentration of tempol in water.

Roehrich A.D., Bordignon E., Mode S., Shen D.K., Liu X., Pain M., Murillo I., Martinez-Argudo I., Sessions R.B, & Blocker A.J. (2016). Steps for Shigella Gatekeeper Protein MxiC Function in Hierarchical Type III Secretion Regulation. The Journal of Biological Chemistry, 292(5), 1705-1723.

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