Tag Archives: xray diffraction

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

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…)

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Revealing the Secrets of Motility in Archaea

Scientists from Berkeley Lab and the Max Planck Institute for Terrestrial Microbiology analyze a unique microbial motor

The protein structure of the motor that propels archaea has been characterized for the first time by a team of scientists from the U.S. Department of Energy’s Lawrence Berkeley National Laboratory (Berkeley Lab) and Germany’s Max Planck Institute (MPI) for Terrestrial Microbiology.

The motility structure of this third domain of life has long been called a flagellum, a whip-like filament that, like the well-studied bacterial flagellum, rotates like a propeller. But although the archaeal structure has a similar function, it is so profoundly different in structure, genetics, and evolution that the researchers argue it deserves its own name: archaellum. (more…)

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Ralph Milliken: Curiosity’s Mission on Mars

As Curiosity, the Mars Science Laboratory rover, gets set to land in the wee hours of Monday morning, Brown geologist Ralph Milliken will be getting ready to get to work. He’s a member of the mission’s science team. His curiosity lies in finding out why Mars is a colder, drier place than it used to be.

PASADENA, Calif. [Brown University] — Ralph Milliken, assistant professor of geological sciences, is on the science team of the Mars Science Laboratory (MSL), which is set to land the rover Curiosity on the Red Planet in the early morning of Aug. 6 Eastern Daylight Time. The rover will allow the team to study the rocks and soils of Gale Crater, giving scientists years of data to help them learn the geological history of the planet. If there are signs of water or organic material, Curiosity can find those, too. (more…)

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Diamond in The Rough: Half-Century Puzzle Solved

A Yale-led team of mineral physicists has for the first time confirmed through high-pressure experiments the structure of cold-compressed graphite, a form of carbon that is comparable in hardness to its cousin, diamond, but only requires pressure to synthesize. The researchers believe their findings could open the way for a super hard material that can withstand great force and can be used — as diamond-based materials are now — for many electronic and industrial applications. The study appears in Scientific Reports, a Nature journal.

Under normal conditions, pure carbon exhibits vastly different physical properties depending on its structure. For example, graphite is soft, but diamond is one of the hardest materials known. Graphite conducts electricity, but diamond is an insulator. (more…)

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A New Way of Looking at Photosystem II

Berkeley Lab and SLAC Researchers Study Key Protein Complex Crucial to Photosynthesis

Future prospects for clean, green, renewable energy may hinge upon our ability to mimic and improve upon photosynthesis – the process by which green plants, algae and some bacteria convert solar energy into electrochemical energy. An artificial version of photosynthesis, for example, could use sunlight to produce liquid fuels from nothing more than carbon dioxide and water. First, however, scientists need a better understanding of how a large complex of proteins, called photosystem II, is able to split water molecules into oxygen, electrons and hydrogen ions (protons). A new road to reaching this understanding has now been opened by an international team of researchers, led by scientists at the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) and SLAC National Accelerator Laboratory.

Using ultrafast, intensely bright pulses of X-rays from SLAC’s Linac Coherent Light Source (LCLS), the research team produced the first ever images at room temperature of microcrystals of the photosystem II complex. Previous imaging studies, using X-rays generated via synchrotron radiation sources, required cryogenic freezing, which alters the samples. Also, to catalyze its reactions, photosystem II relies upon an enzyme that contains a manganese-calcium cluster that is highly sensitive to radiation. With the high-intensity femtosecond X-ray pulses of the LCLS, the research team was able to record intact images of these clusters before the radiation destroyed them. (more…)

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Under the Electron Microscope – A 3-D Image of an Individual Protein

*The high resolution of Lawrence Berkeley National Laboratory’s Gang Ren*

When Gang Ren whirls the controls of his cryo-electron microscope, he compares it to fine-tuning the gearshift and brakes of a racing bicycle. But this machine at the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) is a bit more complex. It costs nearly $1.5 million, operates at the frigid temperature of liquid nitrogen, and it is allowing scientists to see what no one has seen before.

At the Molecular Foundry, Berkeley Lab’s acclaimed nanotechnology research center, Ren has pushed his Zeiss Libra 120 Cryo-Tem microscope to resolutions never envisioned by its German manufacturers, producing detailed snapshots of individual molecules. Today, he and his colleague Lei Zhang are reporting the first 3-D images of an individual protein ever obtained with enough clarity to determine its structure. (more…)

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