804 research outputs found
Measuring the Magnetic Flux Density with Flux Loops and Hall Probes in the CMS Magnet Flux Return Yoke
The Compact Muon Solenoid (CMS) is a general purpose detector, designed to
run at the highest luminosity at the CERN Large Hadron Collider (LHC). Its
distinctive features include a 4 T superconducting solenoid with 6-m-diameter
by 12.5-m-length free bore, enclosed inside a 10,000-ton return yoke made of
construction steel. The flux return yoke consists of five dodecagonal
three-layered barrel wheels and four end-cap disks at each end comprised of
steel blocks up to 620 mm thick, which serve as the absorber plates of the muon
detection system. To measure the field in and around the steel, a system of 22
flux loops and 82 3-D Hall sensors is installed on the return yoke blocks. A
TOSCA 3-D model of the CMS magnet is developed to describe the magnetic field
everywhere outside the tracking volume that was measured with the field-mapping
machine. The voltages induced in the flux loops by the magnetic flux changing
during the CMS magnet standard ramps down are measured with six 16-bit DAQ
modules. The off-line integration of the induced voltages reconstructs the
magnetic flux density in the yoke steel blocks at the operational magnet
current of 18.164 kA. The results of the flux loop measurements during three
magnet ramps down are presented and discussed.Comment: 3 pages, 6 figures, presented at the IEEE Nuclear Science Symposium
2016 (NSS) in Strasbourg, France on November 3, 2016. arXiv admin note: text
overlap with arXiv:1605.0877
Flux Loop Measurements of the Magnetic Flux Density in the CMS Magnet Yoke
The Compact Muon Solenoid (CMS) is a general purpose detector, designed to
run at the highest luminosity at the CERN Large Hadron Collider (LHC). Its
distinctive features include a 4 T superconducting solenoid with 6-m-diameter
by 12.5-m-length free bore, enclosed inside a 10,000-ton return yoke made of
construction steel. The return yoke consists of five dodecagonal three-layered
barrel wheels and four end-cap disks at each end comprised of steel blocks up
to 620 mm thick, which serve as the absorber plates of the muon detection
system. To measure the field in and around the steel, a system of 22 flux loops
and 82 3-D Hall sensors is installed on the return yoke blocks. A TOSCA 3-D
model of the CMS magnet is developed to describe the magnetic field everywhere
outside the tracking volume measured with the field-mapping machine. The first
attempt is made to measure the magnetic flux density in the steel blocks of the
CMS magnet yoke using the standard magnet discharge with the current ramp down
speed of 1.5 A/s.Comment: 7 pages, 5 figures, presented at ISCM2016 - 5th International
Conference on Superconductivity and Magnetism on April 28, 2016 at Fethiye,
Turke
Measuring the Magnetic Flux Density in the CMS Steel Yoke
The Compact Muon Solenoid (CMS) is a general purpose detector, designed to
run at the highest luminosity at the CERN Large Hadron Collider (LHC). Its
distinctive features include a 4 T superconducting solenoid with 6-m-diameter
by 12.5-m-length free bore, enclosed inside a 10000-ton return yoke made of
construction steel. The return yoke consists of five dodecagonal three-layered
barrel wheels and four end-cap disks at each end comprised of steel blocks up
to 620 mm thick, which serve as the absorber plates of the muon detection
system. Accurate characterization of the magnetic field everywhere in the CMS
detector is required. To measure the field in and around the steel, a system of
22 flux-loops and 82 3-D Hall sensors is installed on the return yoke blocks.
Fast discharges of the solenoid (190 s time-constant) made during the CMS
magnet surface commissioning test at the solenoid central fields of 2.64, 3.16,
3.68 and 4.01 T were used to induce voltages in the flux-loops. The voltages
are measured on-line and integrated off-line to obtain the magnetic flux in the
steel yoke close to the muon chambers at full excitations of the solenoid. The
3-D Hall sensors installed on the steel-air interfaces give supplementary
information on the components of magnetic field and permit to estimate the
remanent field in steel to be added to the magnetic flux density obtained by
the voltages integration. A TOSCA 3-D model of the CMS magnet is developed to
describe the magnetic field everywhere outside the tracking volume measured
with the field-mapping machine. The results of the measurements and
calculations are presented, compared and discussed.Comment: 9 pages, 7 figures, 16 references, presented at the III International
Conference on Superconductivity and Magnetism (ICSM-2012), Kumburgaz,
Istanbul, Turkey, 29 April - 4 May 201
Validation of the CMS Magnetic Field Map
The Compact Muon Solenoid (CMS) is a general purpose detector, designed to
run at the highest luminosity at the CERN Large Hadron Collider (LHC). Its
distinctive features include a 4 T superconducting solenoid with 6-m-diameter
by 12.5-m-length free bore, enclosed inside a 10,000-ton return yoke made of
construction steel. The return yoke consists of five dodecagonal three-layered
barrel wheels and four end-cap disks at each end comprised of steel blocks up
to 620 mm thick, which serve as the absorber plates of the muon detection
system. To measure the field in and around the steel, a system of 22 flux loops
and 82 3-D Hall sensors is installed on the return yoke blocks. A TOSCA 3-D
model of the CMS magnet is developed to describe the magnetic field everywhere
outside the tracking volume measured with the field-mapping machine. The
magnetic field description is compared with the measurements and discussed.Comment: 7 pages, 5 figures, presented at 4th International Conference on
Superconductivity and Magnetism 2014, April 27 - May 2, 2014, Antalya,
Turkey. arXiv admin note: substantial text overlap with arXiv:1605.08778;
text overlap with arXiv:1212.165
Gluco-oligomers initially formed by the reuteransucrase enzyme of Lactobacillus reuteri 121 incubated with sucrose and malto-oligosaccharides
<p>The probiotic bacterium Lactobacillus reuteri 121 produces a complex, branched (1 -> 4, 1 -> 6)-alpha-d-glucan as extracellular polysaccharide (reuteran) from sucrose (Suc), using a single glucansucrase/glucosyltransferase (GTFA) enzyme (reuteransucrase). To gain insight into the reaction/product specificity of the GTFA enzyme and the mechanism of reuteran formation, incubations with Suc and/or a series of malto-oligosaccharides (MOSs) (degree of polymerization (DP2-DP6)) were followed in time. The structures of the initially formed products, isolated via high-performance anion-exchange chromatography, were analyzed by matrix-assisted laser-desorption ionization time-of-flight mass spectrometry and 1D/2D H-1/C-13 NMR spectroscopy. Incubations with Suc only, acting as both donor and acceptor, resulted in elongation of Suc with glucose (Glc) units via alternating (alpha 1 -> 4) and (alpha 1 -> 6) linkages, yielding linear gluco-oligosaccharides up to at least DP similar to 12. Simultaneously with the ensemble of oligosaccharides, polymeric material was formed early on, suggesting that alternan fragments longer than DP similar to 12 have higher affinity with the GTFA enzyme and are quickly extended, yielding high-molecular-mass branched reuteran (4 x 10(7) Da). MOSs (DP2-DP6) in the absence of Suc turned out to be poor substrates. Incubations of GTFA with Suc plus MOSs as substrates resulted in preferential elongation of MOSs (acceptors) with Glc units from Suc (donor). This apparently reflects the higher affinity of GTFA for MOSs compared with Suc. In accordance with the GTFA specificity, most prominent products were oligosaccharides with an (alpha 1 -> 4)/(alpha 1 -> 6) alternating structure.</p>
Measurement of the CMS Magnetic Field
The measurement of the magnetic field in the tracking volume inside the
superconducting coil of the Compact Muon Solenoid (CMS) detector under
construction at CERN is done with a fieldmapper designed and produced at
Fermilab. The fieldmapper uses 10 3-D B-sensors (Hall probes) developed at
NIKHEF and calibrated at CERN to precision 0.05% for a nominal 4 T field. The
precise fieldmapper measurements are done in 33840 points inside a cylinder of
1.724 m radius and 7 m long at central fields of 2, 3, 3.5, 3.8, and 4 T. Three
components of the magnetic flux density at the CMS coil maximum excitation and
the remanent fields on the steel-air interface after discharge of the coil are
measured in check-points with 95 3-D B-sensors located near the magnetic flux
return yoke elements. Voltages induced in 22 flux-loops made of 405-turn
installed on selected segments of the yoke are sampled online during the entire
fast discharge (190 s time-constant) of the CMS coil and integrated offline to
provide a measurement of the initial magnetic flux density in steel at the
maximum field to an accuracy of a few percent. The results of the measurements
made at 4 T are reported and compared with a three-dimensional model of the CMS
magnet system calculated with TOSCA.Comment: 4 pages, 5 figures, 15 reference
Selective Pressure for Biofilm Formation in Bacillus subtilis: Differential Effect of Mutations in the Master Regulator SinR on Bistability
Kampf J, Gerwig J, Kruse K, et al. Selective Pressure for Biofilm Formation in Bacillus subtilis: Differential Effect of Mutations in the Master Regulator SinR on Bistability. mBio. 2018;9(5): e01464-18
Enzymatic depolymerization of alginate by two novel thermostable alginate lyases from Rhodothermus marinus
Alginate (alginic acid) is a linear polysaccharide, wherein (1â4)-linked ÎČ-D-mannuronic acid and its C5 epimer, α-L-guluronic acid, are arranged in varying sequences. Alginate lyases catalyze the depolymerization of alginate, thereby cleaving the (1â4) glycosidic linkages between the monomers by a ÎČ-elimination mechanism, to yield unsaturated 4-deoxy-L-erythro-hex-4-enopyranosyluronic acid (Î) at the non-reducing end of resulting oligosaccharides (α-L-erythro configuration) or, depending on the enzyme, the unsaturated monosaccharide itself. In solution, the released free unsaturated monomer product is further hydrated in a spontaneous (keto-enol tautomerization) process to form two cyclic stereoisomers. In this study, two alginate lyase genes, designated alyRm3 and alyRm4, from the marine thermophilic bacterium Rhodothermus marinus (strain MAT378), were cloned and expressed in Escherichia coli. The recombinant enzymes were characterized, and their substrate specificity and product structures determined. AlyRm3 (PL39) and AlyRm4 (PL17) are among the most thermophilic and thermostable alginate lyases described to date with temperature optimum of activity at âŒ75 and 81°C, respectively. The pH optimum of activity of AlyRm3 is âŒ5.5 and AlyRm4 at pH 6.5. Detailed NMR analysis of the incubation products demonstrated that AlyRm3 is an endolytic lyase, while AlyRm4 is an exolytic lyase, cleaving monomers from the non-reducing end of oligo/poly-alginates
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