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Er 5107dq

Manufactured by Bruker
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The ER 5107DQ is an electron paramagnetic resonance (EPR) spectrometer designed for a variety of research applications. It features a high-performance microwave bridge, a temperature-controlled sample cavity, and sensitive detection capabilities. The core function of this product is to enable the analysis and characterization of paramagnetic species in various materials and samples.

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Lab products found in correlation

Elexsys 580, by Bruker (2 mentions) Super q ftu bridge, by Bruker (2 mentions)

2 protocols using er 5107dq

1

Pulsed EPR Measurements of GlpG Enzyme

Check if the same lab product or an alternative is used in the 5 most similar protocols
DEER-EPR measurements were performed on a Bruker Elexsys 580 spectrometer with Super Q-FTu Bridge, Bruker ER 5107DQ resonator and 10 W Q-band amplifier at 80 K. The spin-labeled samples ranging from 80 to 160 μM GlpG were flash-frozen in quartz capillaries using a liquid nitrogen bath immediately prior to data collection. For data collection, 36-ns π-pump pulse was applied to the low field peak of the nitroxide absorption spectrum, and the observer π/2 (16 ns) and π (32 ns) pulses were positioned 17.8 G (50 MHz) upfield, which corresponded to the nitroxide center resonance. A two-step phase cycling (+x, −x) was carried out on the first (π/2) pulse from the observer frequency. The time domain signal collected for each sample varied from 2.3 to 2.5 μs. Based on the collection time, the reliable inter-spin distance range was ~15−~60 Å. DEER data were analyzed using the program LongDistances, which was written in LabVIEW by Christian Altenbach (http://www.biochemistry.ucla.edu/biochem/Faculty/Hubbell/).
Guo R., Gaffney K., Yang Z., Kim M., Sungsuwan S., Huang X., Hubbell W.L, & Hong H. (2016). Steric trapping reveals a cooperativity network in the intramembrane protease GlpG. Nature chemical biology, 12(5), 353-360.
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2

Pulsed EPR Measurements of GlpG Enzyme

Check if the same lab product or an alternative is used in the 5 most similar protocols
DEER-EPR measurements were performed on a Bruker Elexsys 580 spectrometer with Super Q-FTu Bridge, Bruker ER 5107DQ resonator and 10 W Q-band amplifier at 80 K. The spin-labeled samples ranging from 80 to 160 μM GlpG were flash-frozen in quartz capillaries using a liquid nitrogen bath immediately prior to data collection. For data collection, 36-ns π-pump pulse was applied to the low field peak of the nitroxide absorption spectrum, and the observer π/2 (16 ns) and π (32 ns) pulses were positioned 17.8 G (50 MHz) upfield, which corresponded to the nitroxide center resonance. A two-step phase cycling (+x, −x) was carried out on the first (π/2) pulse from the observer frequency. The time domain signal collected for each sample varied from 2.3 to 2.5 μs. Based on the collection time, the reliable inter-spin distance range was ~15−~60 Å. DEER data were analyzed using the program LongDistances, which was written in LabVIEW by Christian Altenbach (http://www.biochemistry.ucla.edu/biochem/Faculty/Hubbell/).
Guo R., Gaffney K., Yang Z., Kim M., Sungsuwan S., Huang X., Hubbell W.L, & Hong H. (2016). Steric trapping reveals a cooperativity network in the intramembrane protease GlpG. Nature chemical biology, 12(5), 353-360.
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