Paul Scherrer Institute

About: Paul Scherrer Institute is a facility organization based out in Villigen, Switzerland. It is known for research contribution in the topics: Neutron & Large Hadron Collider. The organization has 9248 authors who have published 23984 publications receiving 890129 citations. The organization is also known as: PSI.

High resolution X-ray spectroscopy of $\zeta$ Puppis with the XMM-Newton reflection grating spectrometer

Abstract: We present the rst high resolution X-ray spectrum of the bright O4Ief supergiant star Puppis, obtained with the Reflection Grating Spectrometer on-board XMM-Newton. The spectrum exhibits bright emission lines of hydrogen-like and helium-like ions of nitrogen, oxygen, neon, magnesium, and silicon, as well as neon-like ions of iron. The lines are all signicantly resolved, with characteristic velocity widths of order 1000{1500 km s 1 . The nitrogen lines are especially strong, and indicate that the shocked gas in the wind is mixed with CNO-burned material, as has been previously inferred for the atmosphere of this star from ultraviolet spectra. We nd that the forbidden to intercombination line ratios within the helium-like triplets are anomalously low for N VI, O VII, and Ne IX. While this is sometimes indicative of high electron density, we show that in this case, it is instead caused by the intense ultraviolet radiation eld of the star. We use this interpretation to derive constraints on the location of the X-ray emitting shocks within the wind that are consistent with current theoretical models for this system.

Study of the inclusive production of charged pions, kaons, and protons in pp collisions at √s = 0.9,2.76 and 7 TeV

Abstract: Spectra of identified charged hadrons are measured in pp collisions at the LHC for sqrt(s) = 0.9, 2.76, and 7 TeV. Charged pions, kaons, and protons in the transverse-momentum range pt approximately 0.1-1.7 GeV and for rapidities abs(y) < 1 are identified via their energy loss in the CMS silicon tracker. The average pt increases rapidly with the mass of the hadron and the event charged-particle multiplicity, independently of the center-of-mass energy. The fully corrected pt spectra and integrated yields are compared to various tunes of the PYTHIA6 and PYTHIA8 event generators.

Chiral topological semimetal with multifold band crossings and long Fermi arcs

Abstract: Topological semimetals in crystals with a chiral structure (which possess a handedness due to a lack of mirror and inversion symmetries) are expected to display numerous exotic physical phenomena, including fermionic excitations with large topological charge1, long Fermi arc surface states2,3, unusual magnetotransport4 and lattice dynamics5, as well as a quantized response to circularly polarized light6. So far, all experimentally confirmed topological semimetals exist in crystals that contain mirror operations, meaning that these properties do not appear. Here, we show that AlPt is a structurally chiral topological semimetal that hosts new four-fold and six-fold fermions, which can be viewed as a higher spin generalization of Weyl fermions without equivalence in elementary particle physics. These multifold fermions are located at high symmetry points and have Chern numbers larger than those in Weyl semimetals, thus resulting in multiple Fermi arcs that span the full diagonal of the surface Brillouin zone. By imaging these long Fermi arcs, we experimentally determine the magnitude and sign of their Chern number, allowing us to relate their dispersion to the handedness of their host crystal. AlPt is shown to be a chiral topological material with four-fold and six-fold degeneracies in the band structure. Fermi arc edge states span the whole Brillouin zone and their dispersion enables identification of the handedness of the chiral material.

Amyloid fibril systems reduce, stabilize and deliver bioavailable nanosized iron.

Abstract: Iron-deficiency anaemia (IDA) is a major global public health problem. A sustainable and cost-effective strategy to reduce IDA is iron fortification of foods, but the most bioavailable fortificants cause adverse organoleptic changes in foods. Iron nanoparticles are a promising solution in food matrices, although their tendency to oxidize and rapidly aggregate in solution severely limits their use in fortification. Amyloid fibrils are protein aggregates initially known for their association with neurodegenerative disorders, but recently described in the context of biological functions in living organisms and emerging as unique biomaterial building blocks. Here, we show an original application for these protein fibrils as efficient carriers for iron fortification. We use biodegradable amyloid fibrils from β-lactoglobulin, an inexpensive milk protein with natural reducing effects, as anti-oxidizing nanocarriers and colloidal stabilizers for iron nanoparticles. The resulting hybrid material forms a stable protein-iron colloidal dispersion that undergoes rapid dissolution and releases iron ions during acidic and enzymatic in vitro digestion. Importantly, this hybrid shows high in vivo iron bioavailability, equivalent to ferrous sulfate in haemoglobin-repletion and stable-isotope studies in rats, but with reduced organoleptic changes in foods. Feeding the rats with these hybrid materials did not result in abnormal iron accumulation in any organs, or changes in whole blood glutathione concentrations, inferring their primary safety. Therefore, these iron-amyloid fibril hybrids emerge as novel, highly effective delivery systems for iron in both solid and liquid matrices.

Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.

Abstract: Historically, room-temperature structure determination was succeeded by cryo-crystallography to mitigate radiation damage. Here, we demonstrate that serial millisecond crystallography at a synchrotron beamline equipped with high-viscosity injector and high frame-rate detector allows typical crystallographic experiments to be performed at room-temperature. Using a crystal scanning approach, we determine the high-resolution structure of the radiation sensitive molybdenum storage protein, demonstrate soaking of the drug colchicine into tubulin and native sulfur phasing of the human G protein-coupled adenosine receptor. Serial crystallographic data for molecular replacement already converges in 1,000–10,000 diffraction patterns, which we collected in 3 to maximally 82 minutes. Compared with serial data we collected at a free-electron laser, the synchrotron data are of slightly lower resolution, however fewer diffraction patterns are needed for de novo phasing. Overall, the data we collected by room-temperature serial crystallography are of comparable quality to cryo-crystallographic data and can be routinely collected at synchrotrons. Serial crystallography was developed for protein crystal data collection with X-ray free-electron lasers. Here the authors present several examples which show that serial crystallography using high-viscosity injectors can also be routinely employed for room-temperature data collection at synchrotrons.