Vitaly Yakimenko SLAC's Yakimenko guides future of FACET

Growing up in the former Soviet Union, Vitaly Yakimenko says, kids who did very well in school had a choice of two career paths: politics or science. “Science was always more interesting,” says Yakimenko, who recently joined DOE’s SLAC National Accelerator Laboratory as director of FACET, the Facility for Advanced Accelerator Experimental Tests.

He is quick to share another reason for staying on the path of science, one that has deepened over the course of his career: “I enjoy the company of my colleagues. To be surrounded by very smart people most of your life is a rare gift.”

That’s one of the many appeals of SLAC, Yakimenko says, along with strong leadership and the prospect of continuing to work with people who are very knowledgeable, and from whom he expects to learn much.

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The Large Hadron Collider (Photo: CERN)Upgrades extend the reach of the LHC

The Large Hadron Collider, the largest particle accelerator in the world, started colliding particles more than three years ago. Since then, scientists have published more than 700 papers detailing the knowledge they have gained at the cutting edge of particle physics. But much work still lies ahead for the LHC, starting this March with a two-year shutdown during which scientists, engineers and technicians will prepare the machine to run at higher energy.

In the LHC, superconducting magnets steer two beams of protons in opposite directions along a 17-mile ring more than 300 feet beneath the border of Switzerland and France. The beams cross paths in four locations along the ring. When a proton from one beam collides with a proton from the other, the energy of the collision can convert into mass, creating new, massive particles. These particles quickly decay into lighter particles, leaving a whole zoo of particles for scientists to study.

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See also…

DOE Pulse
  • Number 382  |
  • February 18, 2013
  • New look at cell membrane reveals surprising organization

    The local abundance of metabolically incorporated 15N-sphingolipids in the plasma membrane of a fibroblast cell, overlaid on the corresponding secondary electron image. Red and yellow colors are local elevations in sphingolipid abundance. Image by Kevin Carpenter/LLNL. A new way of looking at a cell's surface reveals the distribution of small molecules in the cell membrane, changing the understanding of its organization.

    A novel imaging study by researchers from DOE's Lawrence Livermore National Laboratory, the University of Illinois and the National Institutes of Health revealed some unexpected relationships among molecules within cell membranes.

    Their findings provide a new way of studying cell structure and ultimately its function.

    Led by Mary Kraft of the University of Illinois, Peter Weber of Lawrence Livermore National Laboratory and Joshua Zimmerberg of the National Institutes of Health, the team published their findings in the online version of the Jan. 28 edition of the Proceedings of the National Academy of Sciences.

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  • The motor that drives Archaea

    The motile structures in Bacteria and Archaea. The archaellum (center) functions like a bacterial flagellum but its structure resembles a bacterial Type 4 pilus. The protein structure of the motor that propels Archaea – the third domain of life, along with Bacteria and Eukarya – has been characterized for the first time by a team from DOE’s Lawrence Berkeley National Laboratory and Germany’s Max Planck Institute for Terrestrial Microbiology.

    The researchers, led by Sonja-Verena Albers of the Max Planck Institute and John Tainer of Berkeley Lab’s Life Sciences Division and the Scripps Research Institute, call this unique motor an archaellum. It functions like a bacterial flagellum, a whip-like rotating propeller, but structurally it more closely resembles the Type 4 pilus, the filamentary “grappling hook” by which bacteria attach to surfaces and pull themselves along.

    Genetic modifications of the extremophile S. acidocaldarius in the Albers lab pinpointed the FlaI (“flah-eye”) protein as responsible for assembling the archaellum and making it rotate. Sophia Reindl of Tainer’s lab crystallized the protein and used beamline 8.3.1 at Berkeley Lab’s Advanced Light Source (ALS) to do x-ray crystallography, which revealed that FlaI consists of two parts, a globular base connected to a moveable tip by a flexible linker.

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  • Fuels synthesis insight can reduce costs and greenhouse gases

    Artist’s conception of the process: Researchers open up a component of the biofuel molecule, called a furan ring, to make it easier to chemically alter. Opening these rings into linear chains is a necessary step in the production of energy-dense fuels, so these linear chains can then be converted into alkanes used in gasoline and diesel fuel. Image by Josh Smith, Los Alamos National Laboratory.

    Scientists at DOE's Los Alamos National Laboratory made a major step forward recently towards transforming biomass-derived molecules into fuels. The team elucidated the chemical mechanism of the critical steps, which can be performed under relatively mild, energy-efficient conditions. The journal Catalysis Science & Technology published the research.

    Trash to Treasure

    “Efficient conversion of non-food biomass into fuels and chemical feedstocks could reduce society’s dependence on foreign oil and ensure the long-term availability of renewable materials for consumer products,” said John Gordon, one of the senior Los Alamos scientists on the project.

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  • US toroidal field conductor fabrication advances

    Superconducting strand is cabled at New England Wire Technologies on 2.5 meter wide by 2 meter tall spools before shipment to Florida for conductor jacketing. Photo: NEWT.

    US ITER and its vendors are moving into a new fabrication phase for the toroidal field magnet system in the international ITER fusion reactor. Cabling and conductor fabrication are now underway in New Hampshire and Florida for the niobium-tin wire produced in the US. All of this fabrication effort is in preparation for delivering the final product in 2015 to the European Union.

    As part of its contributions to the ITER project, the United States is producing over 4 miles of cable-in-conduit superconductor; other ITER partners will provide the remainder of the conductor. This conductor will encircle the ITER tokamak in a toroidal pattern, providing immense magnetic fields for confining 150 million degree plasma into a doughnut-like shape.

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