Articles tagged with X Ray Diffraction
Researchers in France have developed a new technique for studying solar panel absorber materials, which could lead to non-toxic and readily available alternatives. The technique involves resonant diffraction of single crystals, allowing for the creation of high-quality material samples.
Researchers have successfully imaged a single layer of proteins using exceptionally bright and fast X-rays, significantly broadening the number and type of proteins that can be studied. This new method, based on XFEL technology, opens up possibilities for understanding protein structures and their role in disease and toxicity.
Researchers used computer simulation to analyze X-ray crystallographic data and found that current software programs underestimate the level of dynamics in proteins. This could lead to more accurate pictures of protein structures and improved development of medicines.
A handheld mineral analyzer has been developed for mining applications, enabling rapid analysis of minerals in the field. The device combines X-ray diffraction (XRD) and X-ray fluorescence (XRF) techniques to identify and quantify minerals within 1-2 minutes.
Researchers at Scripps Research Institute have discovered the atomic-level structure of a genetic defect causing myotonic dystrophy type 2, allowing them to design compounds that improve disease-associated defects in treated cells. The study's findings hold promise for treating this rare form of muscular dystrophy.
Researchers at Scripps Research Institute have developed a new method to map the 3D structure of membrane proteins, including the human serotonin receptor. This approach enables faster and more accurate imaging, potentially condensing the timeline for structural studies from months to days.
Researchers at Stanford and Google have successfully simulated the transformation of a key drug receptor site using Google Exacycle's cloud computing platform. The simulation revealed thousands of possible configurations, providing scientists with a better jumping-off point for computational drug design.
Researchers from Argonne National Laboratory and the University of Washington have identified a method to minimize radiation damage in protein crystals using submicrometer line focusing. This technique enables scientists to collect better data while reducing time and cost associated with repeated experiments.
Researchers have determined the structure of TRPV1, a protein that plays a central role in pain perception and heat sensation, at near-atomic resolution using electron cryo-microscopy. This breakthrough offers fresh insights to drug designers searching for new pain treatments and sheds light on the protein's unique properties.
Researchers at SLAC's Linac Coherent Light Source (LCLS) X-ray laser used the technique to generate an accurate model of lysozyme, a well-studied enzyme found in egg whites. The study opens the door to new discoveries and explores the potential for LCLS to play a leading role in studying important biomolecules of unknown structure.
Scientists have solved the structure of a key protein in the Nipah virus, which could lead to the development of an antiviral drug. The discovery was made by a team at the Scripps Research Institute and found similarities with measles and mumps viruses.
A new aluminum-based alloy has been successfully synthesized, enabling safe and efficient hydrogen storage for fuel cell vehicles. Researchers achieved the goal of creating a simple-structured aluminum-based interstitial alloy through extreme pressure and high temperature conditions.
Researchers studied vanadium dioxide using ALS beamline 4.0.2 to investigate the origin of its metal-insulator transition, which could lead to faster and more energy-efficient electronic devices. The study identified roles for Pi-symmetry and delta-symmetry electron orbitals in controlling the transition.
A team of researchers is studying the protein structure and reaction dynamics of a key photosynthesis catalyst. They aim to understand the intermediate stages necessary for the oxidation of water, which could help develop sustainable solar energy solutions.
Researchers have successfully imaged the changes in morphology of gold nanocrystals under pressures of up to 6.5 gigapascals, solving a long-standing problem in measuring nanomaterial structures. The study shows that the nanocrystals undergo plastic flow, becoming more fluid-like at high pressure, and reveals new insights into the beha...
The Lyncean Compact Light Source is a miniature synchrotron X-ray source that offers high-quality X-ray beams for various applications in biology, chemistry, and materials science. The grant will support further development to enhance its performance.
Berkeley Lab and SLAC researchers demonstrate simultaneous diffraction/spectroscopy of metalloenzymes using ultrafast, intensely bright X-ray pulses. The study provides critical snapshots of the photosystem II machinery's design principles for artificial light-driven catalysts.
Researchers have published a detailed description of neurotensin's interaction with its receptor, suggesting a novel binding mechanism that may activate G-protein coupled receptors. This knowledge could lead to the development of better drugs for conditions such as Parkinson's disease and schizophrenia.
Researchers successfully probed the effects of light on matter at the atomic scale by mixing x-ray and optical light waves. This technique allows them to directly measure how light manipulates chemical bonds in materials, enabling new insights into light-matter interactions.
An international research team has developed a new nanocrystallography technique that captures 3D images of biomolecules in action using the Linac Coherence Light Source X-ray laser. This method allows scientists to study molecules at room temperature without radiation damage, enabling the creation of atomic-scale resolution models.
A team of researchers from Berkeley Lab and SLAC used ultrafast X-rays to produce the first images of photosystem II microcrystals at room temperature. The study reveals new insights into the complex's composition and atomic structure, crucial for understanding its role in photosynthesis.
Scientists used a novel X-ray technique to analyze the structure of hen egg white lysozyme at a high resolution of 0.19 nanometres, demonstrating the potential of free-electron lasers in structural biology. The technique, which uses ultrashort X-ray pulses, enables the study of previously intractable molecular structures.
An international team led by SLAC National Accelerator Laboratory has used the world's most powerful X-ray laser to obtain ultrahigh-resolution views of nano-crystals of biomolecules, including a small protein found in egg whites. This technique enables researchers to view molecular dynamics at a time-scale never observed before.
Scientists have developed a method to analyze noisy X-ray data, revealing details of molecular structure previously discarded due to low signal quality. This breakthrough could lead to more accurate models and improved understanding in biology, medical diagnostics, nanotechnology and other fields.
Researchers at UCLA have developed a new method for directly measuring the atomic structure of nanomaterials, enabling 3D imaging of individual atoms. The technique, known as electron tomography, allows scientists to visualize the interior structure of nanoparticles in unprecedented detail.
Researchers used X-rays to decipher how certain natural antibiotics defy chemical rules, unlocking a mechanism that could enable scientists to synthesize many important chemicals currently found only in nature. The discovery has broad implications, as the six-membered ring is a common structural feature found in hundreds of drug molecu...
Researchers have discovered a way for soil bacteria to convert an epoxide into a six-membered cyclic ether, a common structural feature in hundreds of drug molecules. This breakthrough has implications for the development of new polyether drugs and potential biosynthesis strategies.
Researchers are exploring X-ray imaging as a next-generation tool for gathering detailed structural and functional information on biomolecules. The technology has the potential to surpass traditional X-ray crystallography, enabling the study of complex biological systems in unprecedented detail.
A UC Davis School of Medicine researcher has developed an algorithm that predicts the conformation changes in voltage-gated sodium channels, crucial for designing new drugs to treat chronic pain and epilepsy. This innovation could lead to highly specific and effective therapies with minimal side effects.
Researchers developed a new technique to improve X-ray crystallography, allowing for three to five times better signal levels than standard methods. This enables the study of large molecules with greater depth and understanding while minimizing radiation damage.
Researchers have created a new technique that accurately maps the surface composition of tiny Janus nanoparticles, allowing for better evaluation of their effectiveness in various applications. The breakthrough enables production of cleanly segregated particles, which are potentially more valuable than chemically uniform ones.
Scientists from Spain and France have obtained single-crystal X-ray diffraction images of sepiolite, a lightweight porous mineral used in cat litter. The study opens the path to industrial synthesis and further improvement of its properties, which could lead to edible product applications.
Researchers at Arizona State University developed a new method to determine biomolecule structures, achieving over 3 million clear diffraction patterns with the Linac Coherent Light Source. This milestone has significant potential for discoveries in biology, medicine, clean energy, and the development of targeted cancer drugs.
The February 2011 Geosphere issue explores recent advances in Grenville geology, including pegmatite geochronology and 3D characterization of sandstone using X-ray CT. This themed issue honors James McLelland's contributions to understanding the Grenville Province.
Researchers at the University of Missouri are using X-ray diffraction to study a unique enzyme found in the 'kissing bug' parasite and Aspergillus fumigatus fungus. The goal is to develop drugs that can inhibit the enzyme's activity, which could lead to breakthroughs in treating pulmonary diseases and Chagas disease.
Researchers used femtosecond X-ray powder diffraction to observe the relocation of charges in an ammonium sulfate crystal after photoexcitation. The technique produces a 'molecular movie' of atomic movement at atomic time and length scales.
Researchers at Scripps Research Institute have determined the atomic structure of a human adenovirus, leading to insights into its assembly and potential applications in gene therapy. The largest complex ever solved at atomic resolution, this discovery may lead to more effective treatments for diseases such as cystic fibrosis and cancer.
A team of biochemists has identified the molecular mechanism by which an immune response is triggered by invading viruses, according to recent research. The results could lead to new therapies for viral infections, including the common cold and hepatitis. By understanding how the immune system recognizes viral RNA at the atomic level, ...
Researchers use X-ray diffraction microscope to image the 3D internal structure of yeast spores and cells. The technique overcomes limitations of previous methods, enabling quantitative 3D imaging of whole biological specimens at nanometer-scale resolutions.
Researchers discovered the structure of dynamin, a protein that pinches off tiny pouches from cells' outer membranes, revealing how vesicles form and advancing knowledge of endocytosis. The findings may lead to better ways for delivering drugs.
Researchers at Berkeley Lab's ALS beamline 9.0.1 developed a method to image whole yeast cells with soft X-rays, achieving a resolution of 11-13 nanometers. This breakthrough enables the possibility of full 3D tomography of whole cells at equivalent resolution.
Researchers at Northwestern University discovered that X-rays can drive the formation of a new type of crystal, featuring charged cylindrical filaments. The crystals exhibit striking features, including long-range ordering and high water content, offering new insights into crystallization processes.
Researchers have produced the first images of biological cells using a nanoscale X-ray imaging technique called ptychography. The technique enables accurate maps of electron density in biological samples, which could yield important insights for evolutionary biology and biotechnology.
Researchers from Boston College have made a significant discovery about myelin structure and stability using x-ray diffraction. They found that early protein processes are crucial to the proper formation and layering of the myelin membrane, which is critical for nerve conduction and nervous system function.
A $2.2 million NIH grant will enhance the lab's ability to rapidly detect protein clumps in Alzheimer's and other neurodegenerative diseases using a new high-resolution electron microscope. This technology will also enable researchers to study molecular motors in flagella, leading to a better understanding of these diseases.
New York University chemists have created three-dimensional DNA structures with potential industrial and pharmaceutical applications. The breakthrough uses a technique that organizes matter in six different directions, yielding a 3D crystal structure visible to the naked eye.
Researchers have developed a high-throughput protein pipeline that can analyze 40 proteins in weeks, compared to years with current techniques. This technique allows for the deciphering of extremophiles and better understanding of protein functions.
Researchers from Durham University have successfully mapped the high-resolution structure of the matrix protein, a critical component of enveloped viruses like RSV. This breakthrough could lead to the development of new biochemical tools to treat respiratory ailments and other viral infections.
Scientists have developed a way to train proteins to line up neatly on the surface of water in thin layers called nanofilms. This technique should allow biochemists to better see and study the molecules, leading to new generations of molecular electronics and ultra-thin materials.
Researchers at Rice University have created a precise image of a virus' protective coat, containing 5 million atoms. The image provides the clearest picture yet of the viruses' genome-encasing shell called a 'capsid', which could lead to new approaches for antiviral therapies and gene delivery.
Researchers have gained new insights into the regulation of calpains, enzymes involved in cellular processes and linked to disorders such as muscular dystrophy and Alzheimer's disease. The study reveals how calpastatin attaches to calpain with precise specificity, providing potential targets for drug development.
Researchers have gained insight into how cells accessorize their proteins to regulate function, a process critical for life. By studying the attachment of NEDD8 to cullin-RING, scientists have found that it transforms the enzyme into an activated form that can attach ubiquitin to target proteins.
Researchers have used X-ray diffraction to create the first 3-D images of aerogel structures at nanometer-scale resolution. The study reveals a complex 'blob-and-beam' structure that explains the material's surprising strength and suggests ways to improve its properties.
Researchers at Argonne National Laboratory have developed a method to align large groups of molecules using lasers, allowing for atomic-level resolution imaging without crystallization. This breakthrough could enable the study of thousands of human proteins important for drug interactions.
Researchers at the University of Pittsburgh School of Medicine have deciphered the three-dimensional structure of a membrane-bound enzyme crucial to glycerol metabolism, a vital source of energy. The breakthrough could lead to advances against obesity, diabetes, and other diseases.
Scientists at UAB and Saint Louis University use X-ray crystallography to understand poxvirus infectious potency and how one protein evades the immune system, paving the way for new drug discoveries to combat inflammatory diseases like atherosclerosis and rheumatoid arthritis.
The team led by Maria Schumacher, Ph.D., produced clear 3-D images of the structure resulting from two proteins connecting with a DNA site to 'segregate' DNA during cell division. The solved structure provides fundamental insight into how cells divide with intact DNA.
Scientists have successfully determined the structure of microcrystal grains using a new set-up at the European Synchrotron Radiation Facility. This breakthrough allows researchers to study crystalline structures previously too small to analyze, enabling potential advances in fields like chemistry, physics, and biology.
Researchers can now observe oscillating atoms in an excited bismuth crystal using high-energy X-ray free-electron lasers, revealing new insights into atomic activity. The development of linear accelerator-based X-ray sources holds promise for studying sub-picosecond science and its potential applications in chemistry and biology.
Researchers at St. Jude Children's Research Hospital discovered that a simple chemical link called a thioester bond acts like a switch to control the handoff of a protein called NEDD8 between enzymes E1 and E2. This switch triggers a biochemical cascade that keeps cells alive and functioning normally, including regulating cell division.