Er 4118x md5

Manufactured by Bruker

Sourced in United Kingdom, Germany

The ER 4118X-MD5 is a laboratory equipment product manufactured by Bruker. It is designed for X-band electron paramagnetic resonance (EPR) spectroscopy. The device features a microwave bridge and a magnet system for analyzing samples.

Automatically generated - may contain errors

Lab products found in correlation

Elexsys e580 spectrometer, by Bruker (2 mentions) Itc 503s, by Oxford Instruments (1 mentions) Helium flow cryostat, by Oxford Instruments (1 mentions) Er035m nmr gaussmeter, by Bruker (1 mentions)

Spelling variants of this product

ER 4118X-MD5 resonator (2 citations)

4 protocols using er 4118x md5

X-Band and 140 GHz EPR Spectroscopy

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

X-Band (9 GHz) EPR experiments were
performed using a Bruker ElexSys E580 spectrometer with a Bruker ER
4118X-MD5 dielectric ring resonator employing a cylindrical TE₀₁₁ mode. Sample temperature control was achieved using a Bruker
ER 4118CF-O flow cryostat with liquid helium or liquid nitrogen as
the cryogen and an Oxford Instruments ITC 503S temperature controller.
A custom-built spectrometer was used for 140 GHz EPR experiments.^{92 (link)}

Corzilius B., Michaelis V.K., Penzel S.A., Ravera E., Smith A.A., Luchinat C, & Griffin R.G. (2014). Dynamic Nuclear Polarization of 1H, 13C, and 59Co in a Tris(ethylenediamine)cobalt(III) Crystalline Lattice Doped with Cr(III). Journal of the American Chemical Society, 136(33), 11716-11727.

+ Open protocol

+ Expand

EPR Spectroscopy of Complex I

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

EPR measurements were performed using an X/Q-band Bruker Elexsys E580 Spectrometer (Bruker BioSpin GmbH, Germany) equipped with a closed-cycle cryostat (Cryogenic Ltd., UK) and X-band split-ring resonator module (ER 4118X-MD5), or a Bruker EMXMicro spectrometer with a helium flow cryostat (Oxford Instruments, UK). All measurements were performed at X-band (9.7 GHz). The magnetic field was calibrated at room temperature with a Bruker strong pitch standard (g = 2.0028). Baseline spectra of the empty resonator, of samples containing only buffer, as well as of oxidised complex I were found to be identical; all the CW spectra presented have been baseline subtracted. Continuous-wave EPR measurement conditions were 100 kHz modulation frequency, 7 G modulation amplitude; other measurement conditions are given in figure legends.

Wright J.J., Fedor J.G., Hirst J, & Roessler M.M. (2020). Using a chimeric respiratory chain and EPR spectroscopy to determine the origin of semiquinone species previously assigned to mitochondrial complex I. BMC Biology, 18, 54.

+ Open protocol

+ Expand

Pulsed EPR Spectroscopy for Photoactive Materials

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

CW EPR experiments were performed on an ELEXYS 580 Bruker spectrometer (Ettlingen, Germany) operating at 9.76 GHz, equipped with a Bruker ER 4118X-MD5 resonator housed in liquid helium cryostat from Oxford Inc (Abingdon, Oxfordshire, United Kingdom). The magnetic field was measured with a Bruker ER035M NMR gaussmeter. The spectra were recorded at 10 K and 80 K. The photo-activity of the synthetized material was investigated by means of coupled EPR spectroscopy with in situ irradiation using a Litron Aurora II OPO Laser (Rugby, Warwickshire, United Kingdom). The sample was irradiated for 2 min. EPR spectra were simulated using the Easyspin [53 (link)] software using the function “pepper” and the parameters reported in the main text.

Cerrato E., Privitera A., Chiesa M., Salvadori E, & Paganini M.C. (2022). Nitrogen-Doped Zinc Oxide for Photo-Driven Molecular Hydrogen Production. International Journal of Molecular Sciences, 23(9), 5222.

+ Open protocol

+ Expand

Continuous Wave and DEER EPR Spectroscopy

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

For both CW EPR and DEER experiments, 40% glycerol was added to the spin labeled Tn ternary samples and spectra collected using an ELEXSYS E580 spectrometer (Bruker) with a X-band (9.6 GHz) resonator (ER 4118 X-MD5), as previously described [18] . The protein (100-120 μL of 80-120 μM) was put into 4 mm outer diameter quartz capillaries and snap frozen in liquid nitrogen before inserting into the pre-cooled resonator. The X-band CW experiments were recorded at 150 K with a field sweep of 300 G, 0.2 mW microwave power, and modulation amplitude of 1 G. DEER experiments were recorded at 80 K using a four-pulse sequence with a 2 ms shot repetition time with a 16 ns 90 • pulse. A 32 ns 180 • ELDOR pulse was applied at a frequency detuned from the pulse frequency by 73 MHz to minimize the orientation selection and maximize the fraction of coupled spins.

Kachooei E., Cordina N.M., Potluri P.R., Guse J.A., McCamey D, & Brown L.J. (2021). Phosphorylation of Troponin I finely controls the positioning of Troponin for the optimal regulation of cardiac muscle contraction. Journal of molecular and cellular cardiology, 150.

+ 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!