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Media Contacts
![Snowflakes indicate phases of super-cold ice](/sites/default/files/styles/list_page_thumbnail/public/2019-05/19-G00404_Tulk_PR_0.jpg?h=e4fbc3eb&itok=5fn8aUhP)
An ORNL-led team's observation of certain crystalline ice phases challenges accepted theories about super-cooled water and non-crystalline ice. Their findings, reported in the journal Nature, will also lead to better understanding of ice and its various phases found on other planets, moons and elsewhere in space.
![Samples of 70% dark chocolate prepared for study with the USANS instrument at the Spallation Neutron Source. (Credit: ORNL/Genevieve Martin)](/sites/default/files/styles/list_page_thumbnail/public/2019-05/2018-P05903%20BL-1A%20user%20%20Littrell_Chocolates-0900RR_0.jpg?h=ae1281eb&itok=NuCrKprm)
Tempering, the heating process that gives chocolate its appealing sheen and creamy texture, is a crucial part of crafting quality chocolate. But, at the molecular level, it gets a little tricky, and when done incorrectly, can render entire batches of chocolate gritty and unappetizing.
![Oak Ridge National Laboratory develops liquid helium auto-fill technology](/sites/default/files/styles/list_page_thumbnail/public/2019-05/2019-P02006.jpg?h=1116cd87&itok=D5pb2RTG)
OAK RIDGE, Tenn., May 14, 2019—Advanced Research Systems, Inc., has licensed a technology designed to automatically refill liquid helium used in laboratory equipment for low-temperature scientific experiments, which will reduce downtime, recover more helium and increase overall efficiency.
![Illustration of the intricate organization of the PKA structure, wherein different parts of the protein are connected through elaborate hydrogen bonding networks (dashed yellow lines), glued together by the hydrophobic assemblies (light blue and orange volumes)—all working together to build the functional active site. Insert shows protonation of the transferred phosphoryl group (cyan mesh) and its many interactions with water and the active site amino acid residues. Credit: Jill Hemman/ORNL](/sites/default/files/styles/list_page_thumbnail/public/2019-03/19-G00204_MR_graphic_Kovalevsky_proof5_2.png?h=b7fbb1a9&itok=wrZFNX-o)
OAK RIDGE, Tenn., March 20, 2019—Direct observations of the structure and catalytic mechanism of a prototypical kinase enzyme—protein kinase A or PKA—will provide researchers and drug developers with significantly enhanced abilities to understand and treat fatal diseases and neurological disorders such as cancer, diabetes, and cystic fibrosis.
![Neutron scattering allowed direct observation of how aurein induces lateral segregation in the bacteria membranes, which creates instability in the membrane structure. This instability causes the membranes to fail, making harmful bacteria less effective.](/sites/default/files/styles/list_page_thumbnail/public/2019-03/Neutrons-FightingSuperbugs_0.jpg?h=e4b73f5a&itok=ebOQD-Mr)
As the rise of antibiotic-resistant bacteria known as superbugs threatens public health, Oak Ridge National Laboratory’s Shuo Qian and Veerendra Sharma from the Bhaba Atomic Research Centre in India are using neutron scattering to study how an antibacterial peptide interacts with and fights harmful bacteria.
![To develop complex materials with superior properties, Vera Bocharova uses diverse methods including broadband dielectric spectroscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy; photographer Jason Richards](/sites/default/files/styles/list_page_thumbnail/public/2019-02/2016-p05202.jpg?h=b6236d98&itok=w-Sd8giq)
Vera Bocharova at the Department of Energy’s Oak Ridge National Laboratory investigates the structure and dynamics of soft materials—polymer nanocomposites, polymer electrolytes and biological macromolecules—to advance materials and technologies for energy, medicine and other applications.
![Using neutrons from the TOPAZ beamline, which is optimal for locating hydrogen atoms in materials, ORNL researchers observed a single-crystal neutron diffraction structure of the insoluble carbonate salt formed by absorption of carbon dioxide from the air.](/sites/default/files/styles/list_page_thumbnail/public/2019-02/Carbon_capture_neutrons_0.jpg?h=4137a28c&itok=ZBLNFjNc)
Researchers used neutron scattering at Oak Ridge National Laboratory’s Spallation Neutron Source to investigate the effectiveness of a novel crystallization method to capture carbon dioxide directly from the air.
![Sean Hearne has been named director of the Center for Nanophase Materials Sciences at Oak Ridge National Laboratory. Sean Hearne has been named director of the Center for Nanophase Materials Sciences at Oak Ridge National Laboratory.](/sites/default/files/styles/list_page_thumbnail/public/news/images/2019-P00370.jpg?itok=6sC8Bnj7)
OAK RIDGE, Tenn., Feb. 8, 2019—The Department of Energy’s Oak Ridge National Laboratory has named Sean Hearne director of the Center for Nanophase Materials Sciences. The center is a DOE Office of Science User Facility that brings world-leading resources and capabilities to the nanoscience resear...
![Researchers analyzed the oxygen structure (highlighted in red) found in a perovskite’s crystal structure at room temperature, 500°C and 900°C using neutron scattering at ORNL’s Spallation Neutron Source. Analyzing how these structures impact solid oxide f Researchers analyzed the oxygen structure (highlighted in red) found in a perovskite’s crystal structure at room temperature, 500°C and 900°C using neutron scattering at ORNL’s Spallation Neutron Source. Analyzing how these structures impact solid oxide f](/sites/default/files/styles/list_page_thumbnail/public/Neutron-Fueling_better_power_image1.jpg?itok=tZtIORnX)
A University of South Carolina research team is investigating the oxygen reduction performance of energy conversion materials called perovskites by using neutron diffraction at Oak Ridge National Laboratory’s Spallation Neutron Source.
![ORNL alanine_graphic.jpg ORNL alanine_graphic.jpg](/sites/default/files/styles/list_page_thumbnail/public/ORNL%20alanine_graphic.jpg?itok=iRLfcOw-)
OAK RIDGE, Tenn., Jan. 31, 2019—A new electron microscopy technique that detects the subtle changes in the weight of proteins at the nanoscale—while keeping the sample intact—could open a new pathway for deeper, more comprehensive studies of the basic building blocks of life.