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A Dual Look at Photosystem II Using the World’s Most Powerful X-Ray Laser

By Guest PostFebruary 27, 2013Sciencealgae, berkeley lab, carbon dioxide, catalytic activities, cryogenic temperatures, cyanobacteria, data, earth, energy, free electron laser, green plants, jan kern, junko yano, laser pulses, lcls, light source, linac coherent, living cells, manganese calcium, metal ion, metalloenzyme crystal, metalloenzymes, mn4ca, molecular oxygen, most powerful, natural photosynthesis, nicholas sauter, nitrogen fixation, oxidation states, photo reduction, photon step cycle, photon steps, photosystem, protein complex, proteins, radiation damage, roberto alonso mori, s1 to s4, sensitive to radiation, simulate solar photons, slac, software tools, sunlight, uwe bergmann, vital to life, vittal yachandra, water, water molecules, world, xes, xfel, xray beams, xray diffraction, xray emission spectroscopy, xray laser, xrd

Berkeley Lab and SLAC Researchers Demonstrate Room Temperature Simultaneous Diffraction/Spectroscopy of Metalloenzymes

From providing living cells with energy, to nitrogen fixation, to the splitting of water molecules, the catalytic activities of metalloenzymes – proteins that contain a metal ion – are vital to life on Earth. A better understanding of the chemistry behind these catalytic activities could pave the way for exciting new technologies, most prominently artificial photosynthesis systems that would provide clean, green and renewable energy. Now, researchers with the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) and the SLAC National Accelerator Laboratory have taken a major step towards achieving this goal.

Using ultrafast, intensely bright pulses of X-rays from SLAC’s Linac Coherent Light Source (LCLS), the world’s most powerful X-ray laser, the researchers were able to simultaneously image at room temperature the atomic and electronic structures of photosystem II, a metalloenzyme critical to photosynthesis. (more…)

New Phenomenon in Nanodisk Magnetic Vortices

By Guest PostAugust 12, 2012Scienceals, antisymmetric coupling, atom, cxro, data storage, dzyaloshinskii moriya interaction, eye of hurricane, ferromagnetic nanodisk, hurricane, intrinsic factor, Japan, keisuke yamada, magnetic vortices, magnetism, mi young im, nanodisk, nanoscience, peter fischer, phenomenon, ram, shinya kasai, spin of electrons, symmetry, teruo ono, tomonori sato, xray beams, yoshinobu nakatani

Berkeley Lab Researchers Take a Mesocale Look at Magnetic Vortex Formations

The phenomenon in ferromagnetic nanodisks of magnetic vortices – hurricanes of magnetism only a few atoms across – has generated intense interest in the high-tech community because of the potential application of these vortices in non-volatile Random Access Memory (RAM) data storage systems. New findings from scientists at the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) indicate that the road to magnetic vortex RAM might be more difficult to navigate than previously supposed, but there might be unexpected rewards as well.

In an experiment made possible by the unique X-ray beams at Berkeley Lab’s Advanced Light Source (ALS), a team of researchers led by Peter Fischer and Mi-Young Im of the Center for X-Ray Optics (CXRO), in collaboration with scientists in Japan, discovered that contrary to what was previously believed, the formation of magnetic vortices in ferromagnetic nanodisks is an asymmetric phenomenon. It is possible that this breaking of symmetry would lead to failure in a data storage device during its initialization process. (more…)

Correct Protein Folding:

By Guest PostFebruary 26, 2012Sciencealzheimers, amino acids, atp hydrolysis, atp molecules, biomolecular nanomachines, cancer, chain, chaperonin, corie ralston, crystal structure, diseases, eukaryotes, gold standard, jose pereira, light sources, macromolecules, Nanotechnology, nicholai douglas, nucleotide, parkinson's, paul adams, prokaryotes, protein, ramya kumar, xray beams

*Berkeley Lab Researchers Identify Structure of Key Control Element Behind Protein Misfolding That Can Lead to Disease*

The gold standard for nanotechnology is nature’s own proteins. These biomolecular nanomachines – macromolecules forged from peptide chains of amino acids – are able to fold themselves into a dazzling multitude of shapes and forms that enable them to carry out an equally dazzling multitude of functions fundamental to life. As important as protein folding is to virtually all biological systems, the mechanisms behind this process have remained a mystery. The fog, however, is being lifted.

A team of researchers with the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab), using the exceptionally bright and powerful x-ray beams of the Advanced Light Source, have determined the crystal structure of a critical control element within chaperonin, the protein complex responsible for the correct folding of other proteins. The incorrect or “misfolding” of proteins has been linked to many diseases, including Alzheimer’s, Parkinson’s and some forms of cancer. (more…)

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A Dual Look at Photosystem II Using the World’s Most Powerful X-Ray Laser

New Phenomenon in Nanodisk Magnetic Vortices

Correct Protein Folding: