Emx x band spectrometer

Manufactured by Bruker

Sourced in Germany

The EMX X-band spectrometer is a compact and versatile electron paramagnetic resonance (EPR) spectrometer designed for a wide range of applications. It operates at the X-band frequency range and provides high-sensitivity detection of paramagnetic species. The instrument's core function is to measure and analyze the magnetic properties of materials with unpaired electrons.

Automatically generated - may contain errors

Lab products found in correlation

Dxr raman microscope, by Thermo Fisher Scientific (2 mentions) Esr900 cryostat, by Oxford Instruments (1 mentions) Fp 6500 spectrofluorometer, by Jasco (1 mentions) Lambda 25 spectrophotometer, by PerkinElmer (1 mentions) Bio beads sm 2 adsorbants, by Bio-Rad (1 mentions) Itc 503 temperature controller, by Oxford Instruments (1 mentions) Winepr software, by Bruker (1 mentions) Er 4119hs, by Bruker (1 mentions) Er 041x microwave bridge, by Bruker (1 mentions) Esr900, by Oxford Instruments (1 mentions) Emx instrument, by Bruker (1 mentions) 8453 diode array spectrometer, by Hewlett-Packard (1 mentions) 600d potentiostat, by CH Instruments (1 mentions) Heparin, by Merck Group (1 mentions) Er4102st, by Bruker (1 mentions) Lambda 25 double beam spectrophotometer, by PerkinElmer (1 mentions) J 810 spectropolarimeter, by Jasco (1 mentions) Avance av400, by Bruker (1 mentions) Micro cube, by Elementar (1 mentions) Av250, by Bruker (1 mentions)

35 protocols using emx x band spectrometer

Spin-Trap EPR Detection of Radicals

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

The spin-trap technique revealed the presence of radical species using a X-band Bruker-EMX spectrometer, equipped with a cylindrical cavity operating at 100 kHz field modulation. Experimental parameters were as follows: microwave frequency 9.86 GHz; microwave power 19.97 mW; modulation amplitude 2 Gauss; conversion time 15.43 ms. Spin-traps, 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) or 2,2,6,6-tetramethylpiperidine (TEMP), each 17 mM, were added (separately in different experiments) to the other reagents at t = 0^{44 (link)}.

Farinelli G., Rebilly J.N., Banse F., Cretin M, & Quemener D. (2024). Assessment of new hydrogen peroxide activators in water and comparison of their active species toward contaminants of emerging concern. Scientific Reports, 14, 9301.

+ Open protocol

+ Expand

Detecting Photocatalytic OH• Generation on TiO2

Check if the same lab product or an alternative is used in the 5 most similar protocols

ESR analysis to check the photocatalytic generation of ^•OH on powdered Kronos 1077 TiO₂ and the same sample decorated (Ag-TiO₂) was carried out by using as the irradiating source a solar box (Co. Fo. Megra, Milan, Italy) equipped with a 1500 W Xenon lamp and cut-off filters for wavelengths below 340 nm or 400 nm. Then, 3 mL of a sample suspension (prepared to introduce 100 mg of sample in 100 mL of pure water) were introduced in a quartz cell and irradiated under stirring for 20 min in the presence of 5,5-dimethyl-1-pyrroline-N-oxide (DMPO, 17 mM). ESR spectra were recorded at room temperature using an X-band Bruker-EMX spectrometer equipped with a cylindrical cavity operating at 100 kHz field modulation. Experimental parameters were as follows: microwave frequency 9.86 GHz; microwave power 2.7 mW; modulation amplitude 2 Gauss; conversion time 30.68 ms.

Djellabi R., Basilico N., Delbue S., D’Alessandro S., Parapini S., Cerrato G., Laurenti E., Falletta E, & Bianchi C.L. (2021). Oxidative Inactivation of SARS-CoV-2 on Photoactive AgNPs@TiO2 Ceramic Tiles. International Journal of Molecular Sciences, 22(16), 8836.

+ Open protocol

+ Expand

EPR Spectroscopy of Frozen Protein Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols

Purified proteins were collected in Wilmad Suprasil EPR tubes and gently frozen in liquid N₂ and stored until data acquisition. EPR spectra involved a 5000G sweep on an X-band EMX spectrometer (Bruker Biospin Corp) with a bimodal resonator and cryostat for maintaining a low temperature of 4K. Average microwave frequency, 9.38 GHz; microwave power, 0.2 W; modulation amplitude, 10 G; average time = 300 s. All spectra were normalized and plotted using SpinCount software (http://www.chem.cmu.edu/groups/heindrich). A 1 mM solution of CuSO₄-EDTA was used as a standard.

Khan D., Lee D., Gulten G., Aggarwal A., Wofford J., Krieger I., Tripathi A., Patrick J.W., Eckert D.M., Laganowsky A., Sacchettini J., Lindahl P, & Bankaitis V.A. (2020). A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins. eLife, 9, e57081.

+ Open protocol

+ Expand

EPR Monitoring of TEMPO Redox Reaction

Check if the same lab product or an alternative is used in the 5 most similar protocols

To enhance sensitivity, EPR experiments were performed in organic solvent (MeOH), and therefore, the organic soluble TEMPOL analog, 2,2,6,6-tetramethylpiperidin-1-yl)oxyl (TEMPO) was used. Importantly, the redox potentials for TEMPOL and TEMPO are nearly identical [28 ]. MCPD (5 mM) was added to 10 mL of methanol containing tetrabutylammonium hydroxide (10 mM) and TEMPO (5mM). The EPR spectra were obtained on a Bruker X-band EMX spectrometer with a gun diode as the microwave source running at 9.48 GHz. The TEMPO signal was monitored in an EPR flat cell over time for 100 min at room temperature.

Bianco C.L., Chavez T.A., Sosa V., Saund S.S., Nguyen Q.N., Tantillo D.J., Ichimura A.S., Toscano J.P, & Fukuto J.M. (2016). The Chemical Biology of the Persulfide (RSSH)/Perthiyl (RSS·) Redox Couple and Possible Role in Biological Redox Signaling. Free radical biology & medicine, 101, 20-31.

+ Open protocol

+ Expand

Spectroscopic Analysis of Cellular Components

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

MB, EPR, and UV–vis spectra
were collected and analyzed as described.^{23 (link)} MB spectra were collected using a MS4 WRC spectrometer (SEE Co.,
Edina MN), calibrated using α-Fe foil at room temperature. Spectra
were analyzed and simulated using WMOSS software. EPR spectra were
collected at the University of Texas at Arlington on an X-band EMX
spectrometer (Bruker Biospin Corp., Billerica, MA) equipped with a
bimodal resonator (4116DM) and an Oxford Instruments ESR900 cryostat.
Signals were integrated using a custom Matlab (Mathworks.com) program.
Spin concentrations were calculated as described^{24 (link)} using 1.00 mM CuSO₄-EDTA as the standard.
UV–vis spectra of whole cells were collected on a Hitachi
U3310 spectrometer with a Head-on photomultiplier tube. Spectra were
simulated using OriginPro software as described.^{23 (link)} Packed-cell samples were diluted 3-fold with ddH₂O and analyzed in a 10 mm path length quartz UV–vis cuvette
(Precision cells). After collecting MB spectra, isolated mitochondria
were thawed anaerobically in a glovebox (≤5 ppm of O₂, MBraun, Labmaster), diluted 3-fold with SH buffer (0.6 M Sorbitol,
0.02 M HEPES, Fisher Scientific, pH 7.4), and transferred to a 2 mm
path length quartz UV–vis cuvette (Precision cells). The cuvette
was sealed with a rubber septum and brought out of the glovebox and
immediately analyzed by UV–vis.

Cockrell A., McCormick S.P., Moore M.J., Chakrabarti M, & Lindahl P.A. (2014). Mössbauer, EPR, and Modeling Study of Iron Trafficking and Regulation in Δccc1 and CCC1-up Saccharomyces cerevisiae. Biochemistry, 53(18), 2926-2940.

+ Open protocol

+ Expand

Electron Spin Resonance Spectroscopy Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols

CW spectra were recorded on a Bruker X-band EMX spectrometer with an SHQE resonator. Simulations of fluid solution and rigid lattice spectra were performed with locally-written software that calculates hyperfine splittings to first order. Hamiltonian parameters are summarized in Tables 1 and 2.

Eaton S.S., Rajca A., Yang Z, & Eaton G.R. (2017). Azaadamantyl Nitroxide Spin Label: Complexation with β-Cyclodextrin and Electron Spin Relaxation. Free radical research, 52(3), 319-326.

+ Open protocol

+ Expand

Carrageenan Radiolysis Characterization by ESR

Check if the same lab product or an alternative is used in the 5 most similar protocols

The free radical created in carrageenan rods by radiation in the range of 0.5-130 kGy at room temperature (21-25 0 C) was detected by X-band EMX spectrometer (Bruker, Germany) using a standard rectangular cavity of ER 4102. Samples were inserted in ESR tubes, the bottom of each tube was adjusted at a fixed define position to ensure reproducible and accurate positioning of the rods in the sensing zone of the cavity. The stability of the ESR spectrometer and sensitivity were checked before and after each series of measurements using reference alanine dosimeter. Finally, the dose response curve was established in terms of correlated signal intensity against the absorbed doses. Three prepared carrageenan rods were irradiated at each dose point and analyzed by the ESR spectrometer.

Faheem E., Moniem S.A., & Ahdal m.e. (2020). Preparation of New ESR Dosimetry System for High Dose Radiation Processing. Egyptian Journal of Chemistry, 63(4), 9-10.

+ Open protocol

+ Expand

EPR Spectroscopy of Membrane Protein

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

For EPR measurements, LUVs were formed from POPC:POPS=80:20 in a Ca²⁺ free buffer (20 mM HEPES, 150 mM KCl, pH 7.4) and either 1 mM Ca²⁺ or Cd²⁺ was added as needed. EPR spectra were recorded using a Bruker X-Band EMX spectrometer (Bruker Biospin, Billerica, MA) equipped with an ER 4123D dielectric resonator. All EPR spectra were recorded using a 100 G magnetic field sweep, 1 G modulation, and 2.0-milliwatt incident microwave power at a temperature of 298 K. The measurements were performed on 10-µl samples in glass capillary tubes (0.60 mm inner diameter × 0.84 mm outer diameter round capillary; VitroCom, Mountain Lakes, NJ). The protein concentrations used were approximately 75 µM. The phasing, normalization, and subtraction of EPR spectra were performed using LabVIEW software provided by Dr. Christian Altenbach (UCLA, Los Angeles, CA). Progressive power saturation of the EPR spectrum was used to determine nitroxide membrane depth and was performed as previously described.^{35 (link), 42 (link)} In this case, samples were placed into TPX-2 capillaries, and the values of ΔP_½ obtained in air and in the presence of Ni(II)EDDA were used to calculate a depth parameter, Φ.^{16 (link)} The spin label depth was then estimated using the empirical expression:

Φ = 3.4 tanh (0.11 (x - 8.56)) + 1.1

where x is the distance of the spin label from the phospholipid phosphate plane in the bilayer.^{43 (link)}

Katti S., Nyenhuis S.B., Her B., Srivastava A.K., Taylor A.B., Hart P.J., Cafiso D.S, & Igumenova T.I. (2017). Non-native metal ion reveals the role of electrostatics in Synaptotagmin 1-membrane interactions. Biochemistry, 56(25), 3283-3295.

+ Open protocol

+ Expand

Fibril Formation Analysis by EPR Spectroscopy

Check if the same lab product or an alternative is used in the 5 most similar protocols

Fibril formation was confirmed by measuring Thioflavin T fluorescence at 482 nm (FP-6500 spectrofluorometer, Jasco, Inc., Easton, MD). Fibrils were collected using centrifugation at 13,500 rpm for 10 minutes (5840R centrifuge, F45-30-11 rotor, Eppendorf AG Hamburg, Germany). The soluble portion was removed and the remaining pellet was washed repeatedly with deionized water. The sample was then loaded into a boro capillary tube (0.6 mm inner diameter, 0.84 mm outer diameter, Vitro-Com, Mt. Lakes, NJ).
Continuous wave EPR spectra were collected at room temperature using a Bruker X-band EMX Spectrometer (Bruker Biospin Corporation). Each sample was scanned 15 times using scan width of 150 gauss in an HS cavity and microwave power of 12.60 milliwatts. In a some cases (i.e. residues 10, 12, 23, and 34), spectra of the supernatant were subtracted from the fibril spectra to get cleaner fibril spectra.

Cervantes S.A., Bajakian T.H., Soria M.A., Falk A.S., Service R.J., Langen R, & Siemer A.B. (2016). Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A. Scientific Reports, 6, 38265.

+ Open protocol

+ Expand

Measuring Antioxidant Responses in Plant Roots

Check if the same lab product or an alternative is used in the 5 most similar protocols

Determination of NO in the roots was carried out by electron paramagnetic resonance (EPR) using the NO trap sodium diethyldithiocarbamate (DETC) [21 (link)]. The EPR signal of mononitrosyl iron complexes with DETC in roots treated with spermine was recorded on an EMX X-band spectrometer (Bruker, Bremen, Germany) at a temperature of 77 °K.
The H₂O₂ content in the supernatants of root homogenates was determined spectrophotometrically using the xylenol orange method (Sigma, Shanghai, China) using a Lambda-25 spectrophotometer (PerkinElmer, Waltham, CT, USA, λ₅₆₀). The concentration of H₂O₂ was calculated using a calibration curve [22 (link)]. Lipid peroxidation in the soluble fraction of the homogenate was assessed spectrophotometrically by measuring the content of TBA-reactive products (λ₅₃₂) [23 (link)].

Minibayeva F., Mazina A., Gazizova N., Dmitrieva S., Ponomareva A, & Rakhmatullina D. (2023). Nitric Oxide Induces Autophagy in Triticum aestivum Roots. Antioxidants, 12(9), 1655.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!