Dark matter search in nucleon, pion, and electron channels from a proton beam dump with MiniBooNE

A search for sub-GeV dark matter produced from collisions of the Fermilab 8 GeV Booster protons with a steel beam dump was performed by the MiniBooNE-DM Collaboration using data from $1.86 \times 10^{20}$ protons on target in a dedicated run. The MiniBooNE detector, consisting of 818 tons of mineral oil and located 490 meters downstream of the beam dump, is sensitive to a variety of dark matter initiated scattering reactions. Three dark matter interactions are considered for this analysis: elastic scattering off nucleons, inelastic neutral pion production, and elastic scattering off electrons. Multiple data sets were used to constrain flux and systematic errors, and time-of-flight information was employed to increase sensitivity to higher dark matter masses. No excess from the background predictions was observed, and 90$\%$ confidence level limits were set on the vector portal and leptophobic dark matter models. New parameter space is excluded in the vector portal dark matter model with a dark matter mass between 5 and 50$\,\mathrm{MeV}\,c^{-2}$. The reduced neutrino flux allowed to test if the MiniBooNE neutrino excess scales with the production of neutrinos. No excess of neutrino oscillation events were measured ruling out models that scale solely by number of protons on target independent of beam configuration at 4.6$\sigma$.Comment: 19 pages, 25 figures, Data release: http://www-boone.fnal.gov/for_physicists/data_release/dark_matter_prd/ v2 Updated to published versio

A modified electrode for the electrochemical reduction of isoflurane.

The popular anaesthetic gas isoflurane is found to be electrochemically inert on a wide range of conventional electrode materials in both aqueous and non-aqueous solvents. However the chemically modified electrode produced by depositing the novel electroactive polymer, poly(vinylfluoranthene), onto a platinum electrode is shown to mediate electron transfer to the anaesthetic thus bringing about its electro-reduction and so offers the promise of amperometric electrochemical sensors based on this electrode

Insights into mucopolysaccharidosis I from the structure and action of α-L-iduronidase

Mucopolysaccharidosis type I (MPS I), caused by mutations in the gene encoding α-L-iduronidase (IDUA), is one of approximately 70 genetic disorders collectively known as the lysosomal storage diseases. To gain insight into the basis for MPS I, we have crystallized human IDUA produced in an Arabidopsis thaliana cgl mutant. IDUA consists of a TIM barrel domain containing the catalytic site, a β-sandwich domain and a fibronectin-like domain. Structures of IDUA bound to induronate analogues illustrate the Michaelis complex and reveal a (2,5)B conformation in the glycosyl-enzyme intermediate, that suggest a retaining double displacement reaction employing the nucleophilic Glu299 and the general acid/base Glu182. Surprisingly, the N-glycan attached to Asn372 interacts with iduronate analogues in the active site and is required for enzymatic activity. Finally, these IDUA structures and biochemical analysis of the disease-relevant Pro533Arg mutation have enabled us to correlate the effects of mutations in IDUA to clinical phenotypes