Articles tagged with Protein Crystals
Northwestern University chemists have developed a new approach that replaces traditional trial-and-error methods with intentional design using flexible DNA strands. The strategy enables precise control over protein connections, creating soft, flexible crystals with high structural order. This breakthrough simplifies one of structural b...
Researchers at CUNY ASRC have created peptide-based crystalline solids that can switch between soft layered and stiff honeycomb architectures in response to humidity. These dynamic solids exhibit large, controllable changes in mechanical and optical properties, enabling unprecedented adaptability.
Researchers have developed a device that cuts sample consumption by as much as 97% while producing high-quality structural data for X-ray crystallography. This innovation enables the study of rare proteins and accelerates drug discovery, unlocking new insights into disease mechanisms.
A new AI model called Crystalyze can analyze X-ray crystallography data to determine the structure of powdered crystals. The model was trained on a database of over 150,000 materials and successfully predicted structures for over 100 previously unsolved patterns.
Researchers develop innovative strategy to study reaction dynamics and rapid structural changes in protein crystals, enabling detailed analysis of intermediates. The method holds potential for designing new drugs, catalysts, and enzymatic systems.
A new study reveals specialized proteins can dramatically delay ice crystal formation in extreme cold, paving the way for impossible organ transplants. Cryogenic damage compromises cellular structures, leading to irreversible damage and organ failure.
Researchers developed an innovative bioengineering approach using genetically modified bacteria to incorporate protein cages around protein crystals. This method efficiently produces highly customized protein complexes for specialized applications. The resulting crystals have a core-shell structure with a cubic PhC core covered in five...
Scientists at Tokyo Institute of Technology have engineered protein crystals in bacteria to produce hybrid solid catalysts for artificial photosynthesis. These catalysts exhibit high activity and stability, with the potential to convert CO2 into formate upon exposure to light.
Researchers at Ulsan National Institute of Science and Technology have made a breakthrough in creating ultra-photostable avalanching nanoparticles that can perform unlimited photoswitching. This achievement has significant implications for fields like optical probes, 3D optical memory, and super-resolution microscopy.
Researchers have developed an algorithm that can be used to evaluate measurements at X-ray free-electron lasers, improving the precision of protein film analysis. The new method, called low-pass spectral analysis (LPSA), mitigates errors in protein movement reconstruction, allowing for more detailed information to be extracted from data.
A new method developed by Cornell researchers provides tools to interpret discarded X-ray crystallography data, enabling better understanding of proteins' movement, structure, and function. This breakthrough could lead to designing new drugs targeting specific proteins.
MIT engineers develop a new purification method using bioconjugate-functionalized nanoparticles to rapidly crystallize proteins, reducing the cost of manufacturing protein drugs. The approach has shown promising results in isolating lysozyme and insulin, with faster crystallization times and increased nucleation rates.
A new study uses serial femtosecond X-ray crystallography to reveal the structure of NendoU protein at room temperature. The resulting high-resolution image shows that the protein's flexibility plays a crucial role in its functional mechanism, which is essential for designing antiviral drugs against SARS-CoV-2.
Researchers develop a new method to track disease-carrying mosquitoes by ingesting harmless DNA particles, providing unique fingerprints of information. This innovative approach has the potential to revolutionize mosquito-borne disease surveillance and tracking, offering insights into mosquito movement and hotspots.
Scientists developed a novel cell-free protein crystallization (CFPC) method that allows rapid and direct formation of protein crystals without purification processes. The technique has enabled the analysis of unstable proteins, increasing knowledge of cellular processes and functions.
A new study provides critical insights into the pGC-A membrane receptor, a vital component of cardiovascular regulation. The research offers a clearer understanding of this complex receptor and its signaling mechanisms, paving the way for new anti-hypertensive drugs.
Using nearly two decades of research and ultrabright X-ray beams, scientists have created a detailed structural map of the nuclear pore complex (NPC), a key regulator of cellular operations. The results provide significant implications for understanding disease mechanisms and developing new treatments.
Researchers have determined the structure of a molecule that helps S. pneumoniae take up manganese, a mineral essential for its survival. This finding could aid in designing new drugs to block this pathway and deny the bacteria its manganese supply.
Researchers studied DUT-8, a switchable MOF structure that changes shape in response to guest molecules. The findings improve understanding of switching processes and gas exchange reactions in MOFs, paving the way for targeted development of functional materials.
Scientists at Tokyo Institute of Technology use genetic engineering to produce protein assemblies from protein crystals. They successfully synthesized bundled protein filaments with precise arrangement and control.
Scientists observed disulphide bridge formation in ribosomal exit tunnel during protein synthesis, challenging previous assumptions. The discovery sheds new light on the causes of lens opacities and cataracts, a leading cause of vision loss worldwide.
A team of scientists from Arizona State University developed a microfluidic device that reduces sample size and waste in X-ray crystallographic experiments. The device, validated by publishing results in Nature Communications, allows for the determination of protein structures with high resolution and reduced sample consumption.
Cornell structural biologists develop a new method to capture collective protein motion, revealing subtle breathing motions that direct biochemical function. The technique adds valuable information to regular crystallography experiments.
A new method to produce cheaper, longer-lasting vaccines has been developed using a protein called polyhedrin. Researchers found that PH(1-110) particles stored as dry powder can still generate antibodies after up to twelve months of storage.
Researchers have uncovered the nucleation process behind microbial shells' formation, revealing the role of protein building blocks and their interaction with environments. The study could help scientists design self-assembling nanostructures for various tasks.
The European XFEL has enabled scientists to create molecular movies of ultrafast protein movement, allowing them to observe proteins' physical functioning and enzyme activity in real-time. This breakthrough capability opens the door to answering bigger biological questions and potentially saving lives.
Researchers at Washington State University have identified a new therapeutic target for the treatment of gout, a common type of arthritis that causes episodes of painful and stiff joints. Blocking the signaling molecule TAK1 can suppress inflammation caused by gout, according to the study.
Researchers have engineered protein crystals that can generate magnetic forces many times stronger than previously reported. By introducing these crystals into living cells, scientists can move the cells around with a magnet, offering potential applications in fields such as biotechnology and biomedical engineering.
The new sample holder allows for direct crystallization of proteins on the holder, eliminating the need for transfer and reducing damage risk. This innovation simplifies protein crystallography by grouping up to 24 sample holders onto one plate.
Researchers discovered Charcot-Leyden Crystals are abundant in airway mucus, stimulate immune system and promote inflammation, which can be treated with newly developed antibodies. These antibodies can dissolve the crystals to reduce asthma features.
Scientists at Brookhaven National Laboratory developed a new approach to solve protein structures from tiny crystals, utilizing unique sample-handling and data-assembly techniques. The method enables the study of difficult-to-crystallize cell-surface receptors and other membrane proteins, improving our understanding of health and disease.
Antifreeze proteins, typically preventing ice formation, have also been found to promote its growth at extremely low temperatures. This study, published in the Journal of Physical Chemistry Letters, provides insight into the basic processes of ice formation and suggests potential implications for understanding climate.
Researchers from Bielefeld University and international partners have confirmed two-fold ability of antifreeze molecules to trigger or inhibit ice crystal formation depending on temperature. This discovery challenges the long-held view that antifreeze proteins only inhibit ice crystal growth.
A team from Osaka University has made a groundbreaking discovery using non-cryogenic crystals to analyze protein conformational changes and thermodynamic properties. This breakthrough technique allows for precise temperature control, providing valuable insights into the structure and function of enzymes.
A Japanese team has developed a new technique for manufacturing ultraprecise multilayer focusing mirrors that can achieve X-ray beam sizes of less than ten nanometers. This breakthrough enables high-performance X-ray free-electron lasers (XFELs) with improved quality and intensity.
Scientists have developed a method to construct protein nanotubes from engineered protein crystals, which could accelerate the development of artificial enzymes, nano-sized carriers and delivery systems. The new method, reported in Chemical Science, uses protein crystals as a scaffold for proteins to self-assemble into desired structures.
A team of scientists has uncovered the molecular details of protein crystal nucleation, a process with great medical and scientific relevance. They developed a new methodology to study this elusive system, providing insights into polymorph selection and guiding the crystallization process to produce desired crystal forms.
A new method has been developed to crystallize membrane proteins of any type or size, allowing researchers to elucidate their structure. The technique uses lipid-water mixtures to create self-assembled channels that enable large proteins to be crystallized.
An international team of experts has made a fundamental discovery by transforming amyloid fibrils into crystals, a process previously thought to be impossible. The transformation involves untwisting the fibril to form an elongated, matchstick-like crystal with unprecedented stability.
Researchers at NYU Dentistry have identified two proteins that regulate the formation of pearls, a process that could lead to the development of fracture-resistant materials. These materials could be used in dental implants, aerospace applications, or energy transmission.
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 have solved a key mystery about plant chemistry, discovering how a specific protein signals the plant's circadian rhythm. This finding may enable farmers to grow crops in areas previously unsuitable and allow scientists to make targeted mutations to improve plant adaptation.
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.
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 Tokyo Institute of Technology create porous protein crystals with increased porosity, allowing for the accumulation and storage of exogenous molecules in living cells. The engineered crystals showed high stability and ability to retain fluorescent dyes in live cells.
Researchers used microseeding technique to overcome hemihedral twinning in protein crystals. The method successfully produced untwinned crystals of LigM, leading to improved crystal structure determination.
Researchers from MIPT and JINR use intersecting laser beams to test protein crystal quality and spot peculiar protein features. This method improves the accuracy of detecting small crystals, essential for studying membrane proteins.
Researchers at HZB and Marburg developed an expert system that identifies small molecule fragments bound to proteins in raw X-ray diffraction data. The system has been successfully tested on 364 samples, revealing additional candidates for drug development.
Researchers have created an 'adaptive protein crystal' that exhibits a unique property called 'auxetic', where stretching or compressing the material causes it to thicken or shrink in the opposite direction. This material has potential applications in shock-absorbing materials and body armor.
Japanese researchers grew protein crystals in space using interferometry to measure growth rate and dissolution properties. The results showed an increased growth rate despite expected suppression of solution convection, which may be due to suppressed transport speed of impurity molecules.
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 scientists has discovered that larger crystals of bacteriorhodopsin grow by consuming smaller crystals around them, creating a depletion zone. This phenomenon was observed using fluorescence microscopy over the course of a month, showing how the distribution of protein in the sample changed with time.
Researchers used X-ray crystallography, NMR and simulation to study protein movements in crystals. The results show that proteins continue to produce slight residual movements even when crystallised, which blurs the structures obtained via crystallography.
Researchers at Rockefeller University have detailed the structure of the ion channel Slo2.2, which helps regulate potassium ions and prevent overstimulation in neurons. The discovery sheds new light on how neurons reset after intense activity and could potentially inform treatments for epilepsy and intellectual disabilities.
Researchers at RIKEN Brain Science Institute engineered fluorescent protein that rapidly assembles into large crystals in living cells. Cells actively targeted the crystals for degradation, a process known as autophagy, suggesting potential evolutionary pressure to discourage crystal formation.
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 have made significant discoveries about coenzyme Q and its production pathway, shedding light on mitochondrial function and its link to human diseases. Two new studies published in PNAS and Molecular Cell reveal the biochemical functions of key proteins involved in coenzyme Q synthesis.
Researchers discovered that antifreeze protein-bound ice crystals resist melting even when temperatures warm, leading to potential adverse physiological consequences for the fish. The study also found ice superheating in nature, a phenomenon where internal ice crystals fail to melt at their normal melting point.
The Case Center for Synchrotron Biosciences will assemble cutting-edge Nnew beamlines at Brookhaven National Laboratory, delivering ultra powerful x-rays to visualize nano-scale structures of molecules and proteins. The new facility will enable scientists to pinpoint disease-causing vulnerabilities and target therapeutic interventions.
Researchers discovered that antifreeze proteins found in Antarctic fish also prevent internal ice crystals from melting, leading to potential health issues. The study found that these protein-bound ice crystals resist melting even when temperatures warm, causing superheating.