Hematite is a promising electrode material for solar-powered water splitting—an important reqirement for producing hydrogen fuel with zero emissions. At Beamline 7.0.1, researchers have gained a better understanding of hematite's electronic structure through soft x-ray spectroscopy performed in situ and "operando."

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Building on the recent discovery of a highly mobile two-dimensional electron gas at the interface between two insulating oxides, researchers can now generate and control a two-dimensional gas state on bare insulating oxide surfaces, a capability that may speed the future of oxide electronics.

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Magnetic vortices – hurricanes of magnetism only a few atoms across – have been found to form asymmetrically in ferromagnetic nanodisks. This finding contradicts previous beliefs and poses challenges to using magnetic vortexes in random access memory (RAM) data storage systems.

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Scientists working at the ALS have discovered a new route for proton movement from one molecule to another—a basic step in countless chemical and biological reactions—thereby opening new avenues for research in biology, environmental science, and green chemistry.

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At the ALS, researchers have deciphered the crystal structure of a critical control element within large protein-folding machines (chaperonins). In identifying the nucleotide-sensing loop and its controlling role, the researchers believe they may have opened a new avenue by which modified protein-folding activities could be engineered.

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While ubiquitous in nature, symmetry is not always evident. The first observation of hidden rotational symmetries in a magnetic system gives scientists a toolbox for discovering hidden symmetries in diverse material systems.

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Researchers have turned a benign virus into an engineering tool for assembling structures that mimic collagen, one of the most important structural proteins in nature. The process they developed could eventually be used to manufacture materials with tunable optical, biomedical, and mechanical properties.

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Tri-block copolymers can serve as scaffolds and templates for a vast number of novel and useful nanostructures. Resonant soft x-ray scattering at the ALS, a unique, powerful tool for examining complex, multi-component systems, has revealed a new phase of ABC tri-block copolymer with complicated morphology.

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How a clamp loader, a molecular machine that facilities DNA replication, accomplishes its task of attaching a ring-shaped clamp to a DNA strand has been unknown at the structural level. New structures obtained at the ALS of clamp-loader complexes in action clarify the mechanism of DNA replication.

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So-called "warm dense matter" (neither solid, liquid, gas, nor plasma) tends to be drastically transient and difficult to study in the laboratory. Researchers have now demonstrated that, at the ALS, fast-changing electron temperatures of matter under extreme conditions can be determined with picosecond resolution.

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In genome engineering, a single position within a DNA sequence is altered without affecting the rest of the genetic code. The structure of a new gene-targeting system, the TAL effector nuclease, reveals its mechanism of action and provides crucial details for its future development.

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The high brightness and coherence of the ALS's soft x-rays have enabled a group of scientists, working at Beamline 12.0.2, to use a lensless x-ray method involving iterative mathematical algorithms to view nanometer-scale magnetic structures in an alloy for the first time.

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A new kind of anode has been developed for use in lithium-ion batteries that is eight times as absorbent as current designs, and has maintained its greatly increased energy capacity after many hundreds of charge-discharge cycles.

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In a new twist on Young's classic double-slit experiment, researchers have shown that the double slits can be replaced by electron-emitting diatomic molecules and that traces of electron-wave interference can be directly observed in measurements of the vibrationally resolved photoionization spectra.

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The signal recognition particle (SRP) transfers new proteins around cells. The newly solved crystal structure of SRP in action exposes new information about its structure and mechanism in this essential and highly-conserved process of co-translational protein targeting.

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