Objective: This matched control study was conducted to evaluate the effect of targeted short-form messages or continuing medical education (CME) on fluoroquinolone prescribing among high prescribers.
Methods: A total of 11,774 Medscape healthcare provider (HCP) members prescribing high volumes of fluoroquinolones were randomized into three segments to receive one of three unique targeted short-form messages, each delivered via email, web alerts, and mobile alerts. Some HCPs receiving targeted short-form messages also participated in CME on fluoroquinolone prescribing.
Single-crystal time-of-flight neutron diffraction has provided atomic resolution of H atoms of HO molecules and hydroxyl groups, as well as Li cations in the uranyl peroxide nanocluster U. Solid-state magic-angle-spinning nuclear magnetic resonance (MAS NMR) spectroscopy was used to confirm the dynamics of these constituents, revealing the transportation of Li atoms and HO through cluster walls. H atoms of hydroxyl units that are located on the cluster surface are involved in the transfer of HO and Li cations from inside to outside and vice versa.
View Article and Find Full Text PDFThe electron densities in two analogous dimetallic transition metal compounds, namely, [M2(μ-OH2)((t)BuCOO)4((t)BuCOOH)2(C5H5N)2] (M = Co(1), Ni(2)), were determined from combined X-ray and neutron single-crystal diffraction at 100 K. Excellent correspondence between the thermal parameters from X- and N-derived atomic displacement parameters is found, indicating high-quality X-ray data and a successful separation of thermal and electronic effects. Topological analysis of electron densities derived from high-resolution X-ray diffraction, as well as density functional theory calculations, shows no direct metal-metal bonding in either compound, while the total energy density at the bond critical points suggests stronger metal-oxygen interactions for the Ni system, in correspondence with its shorter bond distances.
View Article and Find Full Text PDFActa Crystallogr D Biol Crystallogr
June 2011
The hydration of the coenzyme cob(II)alamin has been studied using high-resolution monochromatic neutron crystallographic data collected at room temperature to a resolution of 0.92 Å on the original D19 diffractometer with a prototype 4° × 64° detector at the high-flux reactor neutron source run by the Institute Laue-Langevin. The resulting structure provides hydrogen-bonding parameters for the hydration of biomacromolecules to unprecedented accuracy.
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