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Media Contacts
![A nanobrush made by pulsed laser deposition of CeO2 and Y2O3 with dim and bright bands, respectively, is seen in cross-section with scanning transmission electron microscopy. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-06/HAADF-137804_FIRE_scale_0.jpg?h=ea2c671e&itok=8URQqQi6)
A team led by the Department of Energy’s Oak Ridge National Laboratory synthesized a tiny structure with high surface area and discovered how its unique architecture drives ions across interfaces to transport energy or information.
![Polymer self-assembly at the liquid-liquid interface in real time](/sites/default/files/styles/list_page_thumbnail/public/2020-02/descent.png?h=d1cb525d&itok=rz3eSM-H)
OAK RIDGE, Tenn., Feb. 27, 2020 — Researchers at Oak Ridge National Laboratory and the University of Tennessee achieved a rare look at the inner workings of polymer self-assembly at an oil-water interface to advance materials for neuromorphic computing and bio-inspired technologies.
![Illustration of a nitrogen dioxide molecule (depicted in blue and purple) captured in a nano-size pore of an MFM-520 metal-organic framework material as observed using neutron vibrational spectroscopy at Oak Ridge National Laboratory. Image credit: ORNL/Jill Hemman](/sites/default/files/styles/list_page_thumbnail/public/2019-11/19-G00550_MOF_PR.png?h=e4fbc3eb&itok=3cY5NUpo)
An international team of scientists, led by the University of Manchester, has developed a metal-organic framework, or MOF, material
![CellSight allows for rapid mass spectrometry of individual cells. Credit: John Cahill, Oak Ridge National Laboratory/U.S. Dept of Energy](/sites/default/files/styles/list_page_thumbnail/public/2019-10/4CellSightPhoto_0.png?h=67debf3e&itok=fmsxiN_b)
Researchers at the Department of Energy’s Oak Ridge National Laboratory have received five 2019 R&D 100 Awards, increasing the lab’s total to 221 since the award’s inception in 1963.
![The configurational ensemble (a collection of 3D structures) of an intrinsically disordered protein, the N-terminal of c-Src kinase, which is a major signaling protein in humans. Credit: Oak Ridge National Laboratory, U.S. Dept. of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2019-10/Petridis-PNAS-9.19.19-full%5B3%5D.png?h=d2706590&itok=7rUw2wkM)
Using the Titan supercomputer and the Spallation Neutron Source at the Department of Energy’s Oak Ridge National Laboratory, scientists have created the most accurate 3D model yet of an intrinsically disordered protein, revealing the ensemble of its atomic-level structures.
![Researchers explore the surface chemistry of a copper-chromium-iron oxide catalyst used to generate and purify hydrogen for industrial applications. Credit: Michelle Lehman and Adam Malin/Oak Ridge National Laboratory; U.S. Dept. of Energy.](/sites/default/files/styles/list_page_thumbnail/public/2019-07/h2_graphic_v4_16x9.jpg?h=d1cb525d&itok=UXqJIEOH)
Collaborators at the Department of Energy’s Oak Ridge National Laboratory and U.S. universities used neutron scattering and other advanced characterization techniques to study how a prominent catalyst enables the “water-gas shift” reaction to purify and generate hydrogen at industrial scale.
![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.
![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.
![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.