Archive for the ‘2015 Highlights’ Category
Although they don’t currently have as much conductivity, solid-state electrolytes designed for lithium-ion batteries (LIBs) are emerging as a safer alternative to their more prevalent—sometimes flammable—liquid-electrolyte counterparts. A new study conducted at Oak Ridge National Laboratory’s Spallation Neutron Source (SNS), a Department of Energy Office of Science user facility, has revealed promising results that could drastically boost the performance of solid-state electrolytes, and could potentially lead to a safer, even more efficient battery.
Using neutron diffraction techniques via the VULCAN instrument, the team concluded an in-depth study probing the entire structure evolution of doped garnet-type electrolytes during the synthesis process to unravel the mechanism that boosts the lithium-ionic conductivity. Their findings were recently published in the journals Chemistry of Materials and the Journal of Materials Chemistry A.
Neutron measurements at Oak Ridge National Laboratory’s Spallation Neutron Source are giving physicists new insight into the behavior of quantum magnets. A research team led by Young-June Kim from the University of Toronto used neutron spectroscopy to observe a novel type of energy band repulsion in a magnetic insulator. The study adds to scientists’ understanding of quasiparticles, a theoretical concept that describes many particle interactions inside a material.
This work was conducted at SEQUOIA, SNS beam line 17. The team’s results are published in Nature Physics.
What can skyrmions do for you? These ghostly quantum rings, heretofore glimpsed only under extreme laboratory conditions, just might be the basis for a new type of computer memory that never loses its grip on the data it stores. Now, thanks to a research team including scientists from the National Institute of Standards and Technology (NIST),* the exotic ring-shaped magnetic effects have been coaxed out of the physicist’s deepfreeze with a straightforward method that creates magnetic skyrmions under ambient room conditions. The achievement brings skyrmions a step closer for use in real-world data storage as well as other novel magnetic and electronic technologies.
It took a trip to NIST to confirm the skyrmions’ existence. Creating them involves placing arrays of tiny magnetized cobalt disks atop a thin film made of cobalt and palladium; the NIST Center for Neutron Research (NCNR) had just developed a state-of-art polarized neutron reflectometer that was well suited to study their lab results. Working with NCNR scientists, the team used neutrons to see through the disk to spot the skyrmions underneath. The team also captured images of the whirling configurations in the disk array at NIST’s Center for Nanoscale Science and Technology (CNST) and Lawrence Berkeley Laboratory. This work was published in Nature Communications.
To understand diseases like Parkinson’s, the tiniest of puzzles may hold big answers. That’s why a team including scientists from the National Institute of Standards and Technology (NIST) have determined* how two potentially key pieces of the Parkinson’s puzzle fit together, in an effort to reveal how the still poorly understood illness develops and affects its victims.
This puzzle is a tough one because its pieces are not only microscopic but three-dimensional, and can even change shape. The pieces are protein molecules whose lengthy names are abbreviated as GCase and α-syn. The two proteins wrap around each other and take on a complicated shape before attaching themselves to the membrane surface inside a neural cell in a victim’s brain.
To get a better handle on how these proteins operate in the body, the team—which also included scientists from the National Institutes of Health (NIH) and Carnegie Mellon University—came to the NIST Center for Neutron Research (NCNR) to get a picture of how the two proteins combine into a single unit called a complex that interacts with cell membranes. Using techniques including neutron reflectometry, the team teased out the first-ever structural picture of the GCase/α-syn complex, including their shape change. This work was published in Journal of Biological Chemistry.