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 (1→4)-linked β-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 (1→4) glycosidic linkages between the monomers by a β-elimination mechanism, to yield unsaturated 4-deoxy-L-erythro-hex-4-enopyranosyluronic acid (Δ) 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 ∼75 and 81°C, respectively. The pH optimum of activity of AlyRm3 is ∼5.5 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