Articles tagged with X Ray Diffraction
Researchers at Osaka University developed an acid-tolerant green fluorescent protein, Gamillus, that can withstand low pH environments. The protein exhibits superior acid tolerance and nearly twice the brightness of reported GFPs, making it a powerful tool for imaging in acidic organelles.
Researchers from the Institute for Basic Science synthesized four new kinds of stabilized radicals with ferromagnetic properties, opening doors to applications in rechargeable batteries and molecular spintronics. The oxime radicals were stabilized using N-heterocyclic carbenes, a breakthrough in synthesizing organic radicals.
A new experimental setup allows for serial crystallography using broad-spectrum X-rays at synchrotron sources, enabling the study of proteins with smaller samples and shorter exposure times. This method reduces unwanted scattered radiation, making it possible to determine protein structures with high precision.
Scientists at Tokyo Tech have synthesized a new material, SrYbInO4, which exhibits high oxide-ion conductivity and is the first example of pure oxide-ion conductors with a CaFe2O4-type structure. The material has a lower activation energy for oxide-ion conductivity compared to CaFe2O4.
Researchers at Osaka University developed a novel chimeric antibody fragment to aid in the structural determination of 'uncrystallizable' target proteins. The Fv-clasp design improved production compatibility and stability while maintaining binding ability, enabling successful crystallization of biologically important proteins.
Researchers have solved a decades-long puzzle by using synchrotron radiation X-ray source to probe the structural changes in TMTTF PF6. The team found that the transition involves the formation of a two-dimensional Wigner crystal based on electron distribution pattern changes.
Researchers from Eindhoven University of Technology and Queen's University have detailed the structure of a 600-nanometer protein in an Antarctic bacterium, revealing its role in gripping onto ice surfaces. The discovery has potential applications in preventing pathogenic bacteria from attaching to human cells.
Researchers develop method to directly observe dynamic fracture in metals, shedding light on material properties and behavior under stress. The technique enables real-time observation of atomic structure deformation and determination of stress required for fracture.
Researchers at Lawrence Berkeley National Laboratory develop Multi-Tiered Iterative Phasing (M-TIP) algorithm to determine molecular structure from sparse and noisy single-particle diffraction data. This approach reduces the amount of required information, enabling the extraction of more features from limited experiments.
Researchers used 3D printing to create optimized milling jars for X-ray powder diffraction experiments. The new design improves background and angular resolution, reducing scattering from jar walls and milling balls.
Scientists used an X-ray free-electron laser to determine the atomic structure of an intact virus particle on a microchip containing thousands of tiny pores. This new method allows for faster and more efficient analysis, reducing sample material waste.
Researchers at Argonne National Laboratory used X-ray crystallography to solve the structure of Lassa virus glycoprotein, a key component in vaccine development. The study provides valuable insights into how the virus enters human cells, paving the way for the design of an effective vaccine.
A team led by Kathryn Hastie and Erica Ollmann Saphire at The Scripps Research Institute has solved the structure of Lassa virus's surface glycoprotein, a key step in developing a vaccine. The breakthrough provides a blueprint to design a Lassa virus vaccine, which could help combat the deadly arenavirus family.
Researchers developed a new X-ray technique to examine deformations and dislocations in nanoparticles, which affect their properties. The technique, called Bragg coherent diffraction imaging, allows scientists to reconstruct the size and shape of grain defects in three dimensions.
Scientists developed a novel double flow-focusing nozzle to reduce protein crystal consumption in X-ray crystallography. The new device enables stable experimental conditions, increases the rate of high-quality diffraction patterns, and widens the spectrum of biomolecules that can be analysed.
Defective diamonds are transformed into highly perfect nanodiamonds using high-temperature conditions, enabling precision measurement of electromagnetic fields and other variables. This process improves the homogeneity of crystal lattices, paving the way for scalable methods in quantum sensing.
Researchers used high-intensity X-ray pulses to determine the structure of a viral cocoon down to a scale of 0.2 nanometres, approaching atom-scale resolution. The tiny viruses with their crystal casing are by far the smallest protein crystals ever analyzed using X-ray crystallography.
Researchers at Caltech have discovered the molecular basis for protection of a ribosomal protein from cellular degradation, using X-ray crystallography to solve the structure of the bound pair. This finding has potential applications in developing new cancer drugs by preventing tumor growth.
Researchers discovered new properties in lead zirconate, a key material for creating efficient electrolyte-free accumulators. The discovery reveals unique atomic-scale processes that enable structural switching, contributing to significant energy release in a short period.
A collaborative effort demonstrates that the physical properties of SrTiO3 can be changed by a simple electrical treatment, creating the effect known as piezoelectricity. This discovery opens a new chapter for research into new materials and unusual properties.
Scientists have developed haptic interfaces to enhance collaboration and data analysis in X-ray crystallography. The technology enables real-time visualization and classification of experimental crystallization data on a cloud-based database, streamlining the process and reducing manual effort.
Researchers at University of Surrey develop a scalable and low-cost method to fabricate high-quality isolated organic single crystals using spray-printing. This breakthrough enables the production of inexpensive electronics with applications in flexible circuits, medical detectors, sensors, and more.
Researchers use ultrafast X-ray lasers to study photosystem II protein in action, capturing the first high-resolution 3-D view at room temperature. The study reveals that previous theories explaining the mechanisms may be incorrect and opens new avenues for understanding photosynthesis.
Researchers at MIPT and several universities create technology to determine spatial structure of receptor proteins, crucial for human health. By using sulfur atoms and Serial Femtosecond Crystallography, scientists solve the problem of radiation damage, enabling precise analysis of protein structures with a resolution of 1.9Å.
A new crystallization plate, developed at Cornell University's CHESS, has been used in experiments on the SpaceX CRS 8 mission to learn about protein structure. The In-Situ-1 plate overcomes issues with plastic microplates that made it difficult to assess crystal quality.
Researchers at Washington State University have successfully watched a material's crystal structure change in real time, using a new facility at the Argonne National Laboratory. This breakthrough method allows for actual measurement of physical changes and validation of computer simulations.
Researchers at Princeton University have revealed new insights into the mechanism of phenylalanine hydroxylase, a critical liver enzyme for human health. By applying unique approaches combining small-angle x-ray scattering and chromatography, they provided evidence for a model of the active structure of the enzyme.
Researchers have mapped boron compound distribution in a model control rod, helping determine re-criticality risk within the reactor. This finding could inform decommissioning efforts at Fukushima Daiichi Nuclear Plant.
A new 3-D modeling and data-extraction technique can reveal dynamics in protein crystals, improving the clarity of imaging and providing valuable information about protein motions. This approach has potential benefits for pharmaceutical industry and structural biology.
Researchers have developed a new method to determine the structures of nanocrystalline pharmaceuticals, reducing radiation damage and allowing for study at room temperature. The approach uses low-dose electron diffraction with a high-sensitivity detector, enabling the collection of high-quality data for direct crystallography methods.
Researchers used the powerful x-ray pulses from SACLA to investigate excited-state induced transient lattice dynamics in phase-change materials. They observed non-thermal local structural rearrangements within a few picoseconds, followed by warming of the lattice and a 2 pm change in lattice spacing after 20 ps.
Researchers have developed a new method to obtain high-resolution molecular images using continuous diffraction patterns in imperfect crystals. This approach allows for better structural detail and could revolutionize the study of complex biological machinery, including photosynthesis and catalysis.
Researchers develop a new technique to determine the spatial structures of proteins and molecules without prior knowledge, revolutionizing crystallography. The method provides insights into the modes of action of biomolecules and can lead to tailor-made drugs for diseases.
Researchers propose using twisted X-rays to study non-crystalline but symmetric structures like helices. This method matches the symmetry of incoming radiation to the structure's symmetry, producing sharp peaks in diffraction data that can be used for accurate structure prediction.
A team of physicists has identified a material with negative thermal expansion, shrinking in size as it warms. The discovery challenges current theoretical understanding of thermal expansion and may lead to the development of more durable electronics.
Scientists at UCLA used a microscope to image the 3D positions of individual atoms with precision of 19 trillionths of a meter. This breakthrough enables researchers to infer macroscopic material properties from atomic arrangements, guiding the development of aircraft components and other applications.
Researchers use X-rays to study nickelates and discover that tensile strain facilitates the transfer of electrons between atoms, ruling out electronic checkerboard theory. The findings provide new insight into the metal-insulator transition, guiding the design of new electronic devices.
Researchers at SISSA and Elettra Sincrotrone Trieste have used x-ray crystallography to demonstrate that the selectivity filter of ion channels is dynamic, not rigid. This discovery contributes to solving a long-standing debate among biophysicists and neurobiologists.
Researchers observe chemical processes during photographic exposure in real-time, revealing grain rotation and lattice deformation. The technique enables millisecond temporal resolution for investigating dynamic processes in materials.
A novel X-ray lens designed by DESY scientists has been successfully tested, producing sharper and brighter images of the nano world. The lens employs a unique concept to redirect X-rays over a wide range of angles, enabling high convergence power and resolving smaller details.
Fluctuation X-ray scattering measures molecules at short timescales to reveal structural insights into biological molecules and materials. The technique improves upon traditional small-angle X-ray scattering, providing greater detail from limited datasets.
Researchers identify plumbonacrite as intermediate in degradation of red lead, leading to bleaching of the color over time. The discovery sheds new insights into the bleaching process of red lead, revealing a possible reaction pathway involving light and carbon dioxide.
Researchers have successfully imaged the 3D structure of a giant mimivirus using an X-ray free-electron laser, without relying on crystal formation. This achievement paves the way for imaging important pathogenic viruses like HIV and influenza.
A Scripps Research Institute team has discovered an antibody that can target both Marburg and Ebola viruses, paving the way for new treatment options. The antibody works by binding to a vulnerable site on the virus's surface, preventing it from entering human cells.
Scientists have developed a new X-ray source to study how non-addictive painkillers work, revealing the target of binding to neuroreceptors. This breakthrough could lead to designing molecules to generate specific responses and address critical health issues related to opioid abuse.
The new SHELXT program solves the phase problem for single-crystal reflection data using a novel dual-space algorithm, extending resolution and accommodating missing data. With high success rates, it has already solved thousands of structures.
Researchers are developing new software to visualize molecular machines, revealing their inner workings and structures. The Phenix software uses X-ray diffraction spots to create 3-D images of protein molecules.
A research team led by UWM physicists used an ultra-short X-ray pulse to produce
Scientists have developed a new technique to capture the fast dynamics of biomolecules using high-speed X-ray lasers, revealing subtle processes with unprecedented clarity. The study used the photoactive yellow protein as a model system and achieved snapshots of molecular movements at atomic resolution.
Researchers used X-ray laser to capture PYP photocycle with atomic spatial resolution and ultrafast temporal resolution. The study revealed finer details of the cycle, including steps shorter than 1 picosecond.
Researchers developed a comprehensive model to describe photoexcited thin-film lattice dynamics, clarifying the physical and chemical properties of materials. The study used ultrafast X-ray diffraction to analyze the atomic movements in a crystal structure.
Researchers have used X-ray diffraction to investigate photosystem II, revealing structures yet unknown. The results show that photosystem II proteins are arranged within crystals as extended rows, similar to their natural environment.
Researchers have successfully crystallized carbon monoxide bound to the FeMo-cofactor of nitrogenase, a long-sought structure that could reveal the enzyme's mechanism. The breakthrough, achieved by Thomas Spatzal and colleagues, uses optimized crystallization methods and tiny crystal seeds to accelerate growth.
X-ray crystallography has revolutionized our understanding of molecular structures and their influence on various scientific fields. The technique's future holds intriguing possibilities, including potential transformations beyond its current form.
Scientists have determined the 3D structure of 5HT3-R, a receptor involved in conditions like chemotherapy-induced nausea and anxiety. The high-resolution structure reveals the receptor's molecular anatomy, providing insights into its function and potential targets for novel medicines.
Scientists successfully visualize crucial event in photosynthetic reaction, enabling study of protein complex that splits water. This breakthrough uses free-electron laser technique to collect data at room temperature.
Researchers from Umeå University have explored two ways to study the reaction sequence leading to oxygen formation in photosynthesis. The studies used different techniques, including slowing down the reaction and taking X-ray snapshots of the molecule's structure. The results show that small structural changes occur together with proto...
Scientists at Berkeley Lab and SLAC have taken detailed snapshots of the four photon-step cycle of photosynthetic water oxidation in photosystem II. The study provides information that should be useful for designing artificial solar-energy based devices to split water, a crucial step towards clean energy.
Researchers captured the first molecular-level images of photosynthesis, revealing how water is split into oxygen and hydrogen. The breakthrough could lead to the development of artificial systems that mimic and surpass the efficiency of natural photosynthesis.
Researchers used x-ray pulses to trigger superconductivity and reveal the rapid disappearance of 'charge stripes' that hindered it. The findings provide new insights into room-temperature superconductivity and its potential applications in electronics and computation.