Researchers at University of California, San Diego School of Medicine reveal a more accurate structure of Protein Kinase C (PKC), providing new targets to fine-tune the enzyme's activity. The corrected structure suggests ways to turn PKC 'on' for cancer treatment and 'off' for neurodegenerative disease treatment.
Researchers design multicomponent materials by combining molecular and structural properties to form a 3D architecture. The spatial distribution of molecules and electronic properties of building blocks significantly impact optical properties. The study demonstrates the feasibility of using active pharmaceutical ingredients as building...
Researchers at Sanford Burnham Prebys Medical Discovery Institute solved the structure of hypoxia-inducible factors (HIFs), important regulators of tumor response to low oxygen. The findings identify potential targets for new cancer drugs, which could inhibit HIF functions and reduce tumor growth.
Researchers used X-ray crystallography to visualize the structure of a neurotensin receptor, shedding light on its mechanism. Binding of neurotensin to the receptor triggers critical conformational changes that activate G protein-coupled signaling pathways.
A new study led by Dr Kevin Cowtan found that climate models fail to reflect real-world measurements due to using air temperature for the whole globe. With 36 different models recalculated, a third of differences disappeared, leaving remaining discrepancies possibly explained by recent global warming fluctuations
Scientists at Van Andel Research Institute have unraveled the molecular mechanism of TOPLESS, a plant protein that interacts with other molecules to regulate gene silencing. This discovery provides insights into similar pathways in humans and has significant implications for understanding diseases such as cancer.
Researchers at the Henryk Niewodniczanski Institute of Nuclear Physics found that cold crystallization in liquid crystals occurs through two mechanisms: classical thermodynamics and diffusion. The study reveals a wide range of temperatures where cold crystallization can occur, contrary to previous expectations.
The structure of Oskar's two domains has been solved, enabling researchers to understand how the protein functions in developing reproductive cells. The OSK domain binds to RNA, while the LOTUS domain interacts with an enzyme called Vasa helicase, which is crucial for germ plasm formation.
Caltech researchers used ultrafast electron crystallography to visualize changing atomic configurations of phase-change materials. They discovered a previously unknown intermediate atomic state that represents a physical limit to data recording speeds.
Researchers use electron cryo-microscopy to visualize proteasome complex in unprecedented detail, revealing target sites for potential cancer drugs. The study paves the way for more precise and effective treatments.
A new study by TSRI researchers provides a higher-resolution view of the Ebola virus life cycle, revealing key vulnerabilities that can be targeted with antiviral therapeutics. The findings also shed light on how the virus assembles its genetic material, which is critical for understanding its structure-based design.
Researchers have developed new approaches to estimate overall solvent content, model disordered bulk solvent, and identify distinct electron density of ordered solvent molecules in macromolecular crystals. Advanced models are needed to improve understanding of the protein-solvent interface region.
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.
Korean scientists have successfully created a new class of radical compounds by reacting nitric oxide with N-heterocyclic carbenes. The resulting nitric oxide compounds show potential for targeted NO delivery, which could lead to new therapeutic applications in various human diseases.
A recent study has provided a more complete picture of how proteins move, laying the foundation for understanding molecular causes of human disease and developing potent drug treatments.
Researchers at the University of Pennsylvania have developed a new method to recycle rare-earth magnets, simplifying the process and increasing efficiency. The technique uses standard laboratory equipment and can separate neodymium and dysprosium from used electronics in just minutes.
The article explores aperiodic crystals and their implications on our understanding of crystalline order. Recent research has shown that the current definition of crystals, based on point-like diffraction, may need revision as new materials with non-trivial point components in their diffraction are discovered.
Researchers demonstrate a novel approach for generating new phases using high-pressure crystallographic studies of molecular materials. The study reveals the structural changes in α-Co(dca)2 under pressure, shedding light on its correlation with magnetic properties.
Scientists have developed a powerful tool to investigate ion channel selectivity using infrared spectroscopy and molecular dynamic-based simulations. This approach allows for the detection of subtle conformational changes in large membrane proteins, such as potassium channels, at atomic resolution.
Researchers combined powder diffraction data with electron crystallography to solve modulated structures. The technique provides unprecedented detail down to sub-angstrom resolution, improving the reliability of crystal structure investigation.
Researchers Luigi D'Ascenzo and Pascal Auffinger classify 17 carboxyl(ate) motifs in crystal structures using stereochemical considerations. They provide a systematic naming system and implications for crystal engineering, pharmaceutical research, and biomolecular sciences.
Researchers have created tiny gold nanoparticles that exhibit nature's most intricate patterns, marking the first time a nanoparticle of this size has been crystallized and its structure mapped out atom by atom. These patterns are responsible for the high stability of the particles.
Researchers at Texas Biomedical are exploring a novel mechanism for Filovirus detection using llama antibodies, which could lead to more sensitive diagnostic tools for Marburg and Ebola viruses. The goal is to develop streamlined tests that can detect all known and emerging strains of these viruses.
The molecular structure of the cytotoxin from Mycoplasma pneumoniae has been determined, which could lead to the development of effective drugs and vaccines to neutralize its injurious effects. The discovery is a significant breakthrough in understanding respiratory infections such as asthma.
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 investigated MDMA's behavior under extreme pressure, finding no change in polymorph despite elevated pressures. The study suggests that non-hydrostatic conditions may lead to a polymorphic change.
A study published in Nature Structural & Molecular Biology reveals that human DNA polymerase theta may be a promising drug therapy target for inhibiting breast cancer. The researchers used X-ray crystallography to determine the first crystal structures of POLQ, providing insights into its role in DNA repair and genomic instability.
Researchers have discovered a protein in halophilic microbes that can selectively bind to caesium ions, providing potential for bioremediation of radioactive isotopes. The team plans to engineer this protein into plants to absorb and extract caesium from contaminated soil.
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.
The study provides high-resolution pictures of two closely related enzymes, lysosomal phospholipase A2 (LPLA2) and lecithin-cholesterol acyltransferase (LCAT), which play crucial roles in metabolizing cholesterol and other lipids. The findings offer new insights into the mechanisms underlying these disorders and suggest potential thera...
Researchers have developed a novel nucleating agent that improves crystal quality for reluctant proteins and boosts the probability of success in high-throughput trials. The modified molecularly imprinted polymer (MIP) is suitable for automated optimization, making it a potent tool for structural biologists.
Researchers are creating a synthetic vaccine that mimics the structure of the live virus to provide a quicker, easier, and safer alternative. The goal is to eradicate polio without the danger of accidental release associated with traditional vaccines.
Scientists at the University of Oxford have built a complete model of the outer envelope of an influenza A virion using a coarse-grained molecular dynamics simulation. The simulation reveals various characteristics about the membrane components, including the separation of spike proteins and their interactions with host cells. This res...
Researchers have clarified the compound's phases, thermal expansion and hydrogen bonds, shedding new light on its properties. The study uses advanced methods to determine the crystal structure and electronic structure of ammonium carbonate monohydrate.
Researchers found no knots in RNA structures among 6,000 known chains. Instead, naturally occurring RNAs tend to form simple geometric configurations.
Researchers at Cold Spring Harbor Laboratory have discovered a new quality control mechanism where RNAs proofread themselves, ensuring proteins are made correctly. The CCA-adding enzyme uses a screw-like motion to add CCA groups to tRNAs, and the RNA itself determines whether to allow further additions.
Researchers at Scripps Research Institute have identified drug candidates targeting biological pathways involved in brain cell destruction in Parkinson's disease. The new compounds selectively inhibit JNK kinases, which play a central role in the disease, and show promise as potential therapeutics.
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.
A team of researchers at Georgia State University has made groundbreaking discoveries in the tryptophan kynurenine pathway, a metabolic pathway linked to psychiatric and neurodegenerative disorders. The study reveals an unexpected enzymatic activity that could lead to new drug design for these diseases.
Researchers found a class of compounds that could be effective in combating infections caused by enterovirus D68, which has been linked to polio-like symptoms. The study used X-ray crystallography to learn the structure of the virus and an anti-viral compound called pleconaril.
Researchers have identified how PF74 and CPSF6 molecules bind to HIV-1's capsid, preventing its disassembly. This process can be targeted for therapeutic purposes in HIV-1 infections, potentially blocking viral replication.
The Curiosity rover has taken samples of Martian rocks and soils using the CheMin instrument, which has provided insights into processes on Mars. The analysis reveals a complex mineralogy, including aqueous alteration and hydrated sulphates.
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.
Scientists discovered that SPLUNC1 binds to pulmonary lipids to fight lung infection, keeping airways flexible and hydrated. This finding brings the protein closer to becoming a viable therapy for asthma and COPD patients.
Researchers successfully analyzed all known complete proteomes using X-ray crystallography and homology modeling, covering 25% of protein clusters. The study highlights the potential for knowledge-based target selection to increase structural model production, particularly in eukaryotes and archaea.
Researchers used time-lapse crystallography to show that DNA polymerase inserts damaged molecules into DNA strands, triggering cell death in response to environmental exposures. This process can lead to various human diseases, including cancer, diabetes, and cardiovascular disease.
Scientists have determined the complete structure of the influenza virus polymerase, a key machine that makes copies of the virus' genetic material and reads out instructions. The high-resolution structure reveals how the polymerase works as a whole, providing new insights into its function and potential targets for drug design.
The structure determination of a lipid scramblase reveals a novel protein architecture that enables the transport of lipids across cell membranes. The discovery provides insight into the activation of the protein by calcium and has implications for understanding previously unknown mechanisms of lipid transport.
Researchers at RIKEN developed a new technique to analyze protein structures by suspending crystals in a greasy substance, enabling the use of smaller samples and faster data collection. This breakthrough could lead to improved understanding of dangerous proteins, such as those containing mercury.
Researchers from RIKEN found that a subtle change in the Lon enzyme allows bacteria to quickly adapt between low-oxygen gut environments and high-oxygen outside conditions. This discovery could lead to new therapeutic targets for enteric diseases.
The MAX IV facility in Lund, Sweden is developing a storage-ring synchrotron system that will enable new experiments requiring high source brightness and transverse coherence. The system's design challenges include compact magnets and low-vacuum chambers, which require innovative solutions to overcome technical issues.
Biologists at Scripps Research Institute have described the atomic-level workings of microRNA molecules, which control gene expression in all animals and plants. The findings will help guide the development of therapies that harness microRNA's power to regulate key biological processes.
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.
Researchers design manmade proteins with new structures, including central cavities, to enhance biological functions and create novel molecules. The discovery is part of the growing field of synthetic biology at the University of Bristol.
Ines Ehrnstorfer's research reveals the structural basis of DMT1's selective iron and manganese binding. The study shows that mutations weaken ion binding and transport in human DMT1, providing a basis for developing inhibitors to treat iron storage diseases.
A group of scientists from the US used atomic-resolution Z-contrast imaging and X-ray spectroscopy to analyze two types of dislocations in CdTe, a binary II-VI semiconductor. The study could lead to improved conversion efficiency in CdTe solar cells and advance understanding of crystal structure defects.
Scientists at the University of Manchester have identified a novel process for lowering pollutant toxicity using vitamin B12, offering new hope for combating hazardous substances. The research builds on 15 years of investigation into natural organisms that can detoxify pollutants.
A new crystallographic technique enables time-resolved crystallography, allowing researchers to study how molecular structures work. This breakthrough is expected to provide a major boost in areas of research that rely on understanding molecule function.
Advances in X-ray technology enabled refinement of previously intractable proteins like the ribosome and viruses. The Deformable Elastic Network (DEN) approach optimizes protein structure prediction by adjusting features to fit diffraction data, reducing ambiguities.