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Eip model 625a cw frequency counter

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The EIP model 625A CW frequency counter is a compact and versatile instrument designed to measure the frequency of continuous-wave (CW) signals. It provides accurate and reliable frequency measurements up to 26.5 GHz, making it suitable for a wide range of applications.

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Lab products found in correlation

J 715 spectropolarimeter, by Oxford Instruments (3 mentions) Sm 4000 8t magnetocryostat, by Oxford Instruments (3 mentions)

4 protocols using eip model 625a cw frequency counter

1

Anoxic EPR Spectroscopy of Protein

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Protein samples (67 μM) in HEPES buffer (10 mM, pH 7.5 at 25°C) with 55% glycerol were prepared for EPR studies under anoxic conditions in an anaerobic chamber and immediately frozen in liquid N2. EPR spectra were obtained using a Bruker ESP 300E spectrometer fitted with a Varian EIP model 625A continuous wave counter. Samples were kept at 10 or 20 K (see figure captions) using an Oxford ESR 900 continuous flow liquid He cryostat that was regulated by an Oxford ITC4 temperature controller. The microwave frequency was measured using a Varian EIP model 625A CW frequency counter and the following instrument settings were used: frequency = 9.38 GHz, microwave power = 0.1262 mW, gain = 90 dB, modulation amplitude = 4–6 G, modulation frequency = 100 kHz, conversion time = 40.96 ms, time constant = 327.68 ms, range = 1000–4000 G, resolution = 4096 points, averaged = 3 scans Spin quantitation data was collected at 10 or 20 K for each signal and the power varied to obtain a saturation curve. EPR data were fitted using the Easy Spin92 (link) software and double integration of simulated data was performed using IGOR version 6.3 (WaveMetrics).
Tavares N.K., Stracey N., Brunold T.C, & Escalante-Semerena J.C. (2019). The L-Thr kinase/ L-Thr-phosphate decarboxylase (CobD) enzyme from Methanosarcina mazei Gö1 contains metallocenters needed for optimal activity. Biochemistry, 58(30), 3260-3279.
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2

Magnetic Circular Dichroism and EPR Spectroscopy

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Magnetic
circular dichroism (MCD) spectra
were collected on a Jasco J-715 spectropolarimeter in conjunction
with an Oxford Instruments SM-4000 8T magnetocryostat. All MCD spectra
were obtained by taking the difference between spectra collected with
the magnetic field oriented parallel and antiparallel to the light
propagation axis to remove contributions from the natural CD and glass
strain. X-Band EPR spectra were obtained by using a Bruker ESP 300E
spectrometer in conjunction with an Oxford ESR 900 continuous-flow
liquid helium cryostat and an Oxford ITC4 temperature controller.
The microwave frequency was measured with a Varian EIP model 625A
CW frequency counter. All spectra were collected using a modulation
amplitude of 10 G and a modulation frequency of 100 kHz. EPR spectral
simulations were performed using the WEPR program developed by F.
Neese.
Pallares I.G., Moore T.C., Escalante-Semerena J.C, & Brunold T.C. (2014). Spectroscopic Studies of the Salmonella enterica Adenosyltransferase Enzyme SeCobA: Molecular-Level Insight into the Mechanism of Substrate Cob(II)alamin Activation. Biochemistry, 53(50), 7969-7982.
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3

Magnetocryogenic Spectroscopic Analysis

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MCD and low-temperature Abs spectra were collected on a Jasco J-715 spectropolarimeter in conjunction with an Oxford Instruments SM-4000 8T magnetocryostat. All MCD spectra presented herein were obtained by taking the difference between spectra collected with the magnetic field oriented parallel and antiparallel to the light propagation axis to remove contributions from the natural CD and glass strain. X-band EPR spectra were obtained by using a Bruker ESP 300E spectrometer in conjunction with an Oxford ESR 900 continuous-flow liquid helium cryostat and an Oxford ITC4 temperature controller. The microwave frequency was measured with a Varian EIP model 625A CW frequency counter. All spectra were collected using a modulation amplitude of 10 G and a modulation frequency of 100 kHz. EPR spectral simulations were performed using Dr. Mark Nilges’s SIMPOW program.44
Pallares I.G., Moore T.C., Escalante-Semerena J.C, & Brunold T.C. (2016). Spectroscopic studies of the EutT adenosyltransferase from Salmonella enterica: Mechanism of four-coordinate Co(II)Cbl formation. Journal of the American Chemical Society, 138(11), 3694-3704.
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4

Spectroscopic Analysis of EutT Enzyme

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Low-temperature Abs and MCD spectra were collected on a Jasco J-715 spectropolarimeter in conjunction with an Oxford Instruments SM-4000 8T magnetocryostat. All reported MCD spectra were obtained by taking the difference between spectra collected with the magnetic field oriented parallel and antiparallel to the light propagation axis to remove contributions from the natural CD and glass strain. If appropriate, the temperature-independent contributions to a given MCD spectrum were removed by subtracting the spectrum obtained at 25 K from the low-temperature spectrum.
Variable-temperature variable-field (VTVH)-MCD data were obtained at three different wavelengths corresponding to the peak positions of the most intense features in the MCD spectrum of EutTWT/Co. The experimental data were fit as described elsewhere.28 X-band EPR spectra were obtained by using a Bruker ESP 300E spectrometer in conjunction with an Oxford ESR 900 continuous-flow liquid helium cryostat and an Oxford ITC4 temperature controller. The microwave frequency was measured with a Varian EIP model 625A CW frequency counter. All spectra were collected using a modulation amplitude of 10 G and a modulation frequency of 100 kHz. EPR spectral simulations were performed using the SIMPOW6 program.29
Pallares I.G., Moore T.C., Escalante-Semerena J.C, & Brunold T.C. (2017). Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Evidence for a Tetrahedrally Coordinated Divalent Transition Metal Cofactor with Cysteine Ligation. Biochemistry, 56(2), 364-375.
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