Articles tagged with Cryo Electron Microscopy
Researchers at UBC have discovered a key vulnerability across all major COVID-19 variants that can be targeted by neutralizing antibodies. The 'master key' identified is the antibody fragment V H Ab6, which effectively neutralizes SARS-CoV-2 by attaching to the epitope on the spike protein.
Researchers uncovered the sophisticated mechanism of bacterial Tc toxin's action by utilizing cryo-EM and protein NMR 3D snapshots. The subunits assemble like a syringe, triggering the release of toxic enzymes that disturb cytoskeleton regulation, leading to paralysis.
Researchers discovered that CAMSAP2 proteins utilize phase separation to form an 'aster' structure, which then organizes into a microtubule network. This process is crucial for the formation of specialized cell shapes, such as those found in heart muscle and nerve cells.
New study reveals how GABA A receptor antibodies inhibit neurotransmitter binding, leading to hyperexcitability and symptoms like twitching and seizures. The findings pave the way for developing effective therapies and further investigations into other diseases.
A research team led by Professor Youdong Mao has developed a new method using time-resolved cryo-electron microscopy and machine learning-based 4D reconstruction to visualize the USP14-proteasome system in atomic detail. This reveals a 'multiverse' of parallel reality pathways, allowing for targeted inhibition of cancer cells.
A team of researchers has combined expansion microscopy and stimulated Raman scattering microscopy to create a new imaging technique called MAGNIFIERS. This allows for the high-resolution imaging of biomolecules, including proteins, lipids, and DNA, at the nanoscale.
Researchers from Max Planck Institute have determined the 3D structural details of the human CCAN complex, highlighting its unique features and implications for interactions with centromere protein A. This discovery raises fundamental questions about creating artificial chromosomes.
Researchers find NLRP3 protein forms filament that grows in one direction, allowing for targeted treatment of chronic inflammatory diseases. The discovery could potentially stop inflammation at the 'growing end', bringing relief to those suffering from conditions like Alzheimer's disease.
Researchers have developed a new approach to studying RNA molecules using nanotechnology and cryo-electron microscopy (cryo-EM), enabling the analysis of RNA subunits with unprecedented resolution. This breakthrough has significant implications for fundamental research, drug development, and RNA therapeutics.
The study reveals the structure of D13 and its role in assembling into a protein scaffold, which is critical for virus replication. The researchers discovered two ways the proteins interact to form a spherical honeycomb lattice, with a small helix structure playing a key role in assembly.
Researchers used new techniques to uncover the Tetrahymena electron transport chain, revealing gaps in our knowledge of a major branch of life. The study highlights the power of structural biology and shows potential as a discovery tool for biodiversity research.
Researchers at Van Andel Institute have discovered a new, detailed molecular structure of PhyB, a vital photoreceptor in plants, which allows them to sense light and regulate their lifecycles. The findings may lead to breakthroughs in agricultural and bioengineering practices.
Scientists at Van Andel Institute and Rockefeller University have revealed the structure of the 911 DNA checkpoint clamp, which loads onto DNA to repair damage. The novel finding shows that the 911 clamp is loaded onto DNA from the opposite end, a surprise in the field of DNA replication.
Researchers at La Jolla Institute for Immunology have developed two human antibodies that target Ebola virus and Sudan virus, showing promise for a powerful antiviral therapy. The antibodies, 1C3 and 1C11, can block three glycoprotein sites on the virus at once and target the fusion machinery used by the viruses to infect host cells.
Researchers have discovered how bacteria clean up after molecular crashes, revealing a universal rescue mechanism that works in both bacteria and yeast. The study identifies a molecule called SmrB as the key player in this process.
Researchers discovered that bacteria suppress membrane protein transport in response to stress, using alarm hormones to regulate the process. This allows the microorganisms to slow down their cellular processes and recover when conditions become more favorable.
A team of scientists from Martin-Luther-University Halle-Wittenberg and the Max Planck Institute discovered the essential final step in mRNA production. The process involves 16 proteins that precisely control the structure of mRNA, which determines protein function and disease risk.
Researchers from the Max Planck Institute have obtained the first high-resolution 3D image of the muscle protein nebulin using electron cryo-tomography. The structure reveals that each nebulin repeat binds with an actin subunit, acting as a ruler to dictate filament length and interacting with neighboring actin subunits to stabilize it.
Researchers have developed an AI-based method to analyze cryo-electron microscopy data, enabling the simultaneous examination of multiple protein complexes in cells. This breakthrough can lead to a better understanding of protein functions and potentially create new treatments for diseases like Alzheimer's and cancer.
Scientists at Stanford University and SLAC National Accelerator Laboratory have created a molecular cage to study the structure of KIX, a protein used by AML cancer cells. The technique has successfully imaged KIX with cryo-EM, revealing new insights into its function and potential targets for therapy.
Researchers have gained a deeper understanding of how bacteria use the type VI secretion system to develop toxins for battle. The discovery reveals that toxins are encapsulated in a capsule secured by a cork-like plug, which can be released upon mechanical force.
Researchers have discovered a new type of tiny propeller used by archaea, with implications for human health and technology. The study found that the filament is made up of thousands of copies of two alternating proteins, enabling it to move and propel the cell at high speeds.
Scientists at the University of Münster and Max Planck Institute have clarified the molecular basis for cellular degradation processes by elucidating the 3D structure of Mon1/Ccz1. The complex determines which vesicles deliver their content to the lysosome, a key step in protein regulation.
Researchers have solved a decade-long mystery about the PINK1 protein, which plays a critical role in early onset Parkinson's disease. The discovery provides an unprecedented view of the protein and its activation process, paving the way for developing therapeutic agents that could slow or stop the progression of Parkinson's disease.
Researchers have determined the molecular structure of TDP-43 aggregates extracted from human brains, shedding light on its role in neurodegenerative diseases like ALS. The discovery may lead to the development of targeted therapies and diagnostic tests.
Scientists have uncovered the structure of a Black Widow neurotoxin using cryo-electron microscopy, which could lead to the development of an antidote and new pesticides. The findings are a major breakthrough in understanding the molecular mechanism of the toxin.
Researchers have discovered that specific regions of HAT family proteins determine which amino acids they bind to, leading to unique functions in cell growth and diseases like cancer and neurodegenerative disorders. This knowledge will enable efforts to develop compounds targeting these proteins for therapy.
Researchers from the University of Chicago used cryo-electron microscopy to study protein degradation in yeast, describing the structure of a key enzyme involved in ubiquitination. The study provides new insights into the process and its potential role in human diseases such as aging and neurodegeneration.
Scientists at the Max Planck Institute have uncovered how ExoY toxin becomes activated in human cells by binding to actin filaments, leading to devastating enzymatic activity. This discovery sheds light on a crucial molecular mechanism that underlies the pathogenicity of various toxins.
Researchers at Arizona State University have refined cryogenic electron microscopy to produce more accurate structures of biological samples. The new method uses a statistical approach to model transitory structures, which can play a vital role in biological processes.
A global collaboration has identified three groups of antibodies resistant to mutations in the SARS-CoV-2 Spike protein, which could target vulnerable sites on the protein. The study provides a framework for selecting durable antibody cocktails for COVID-19 treatment and will guide the development of more effective antibody therapies.
Researchers have developed a new method for preparing cryo-electron microscopy samples using liquid nitrogen, which cools at rates roughly 50 times slower than ethane. This results in sharper images with reduced beam-induced motion and simplified workflows.
Researchers have mapped the structure of CRISPR-Cas12j3 from bacteriophages, a discovery that reveals how it works and solves packaging problems for genome editing. The new system has vast potential for precise genome editing with improved efficiencies and alternative targeting mechanisms.
Researchers reveal the molecular mechanism of membrane-tethered protein synthesis in human mitochondria, shedding light on its dynamic structure and function. The discovery could explain how mitochondrial disorders such as deafness and cancer develop.
Researchers developed a novel grid to minimize sample movement in single-particle cryo-EM, resulting in higher image quality and increased data throughput. The new support film, dubbed 'hexAuFoil,' reduces particle displacement and enables the collection of clearer protein structures.
A team of Michigan State University scientists developed a reliable model to study giant viruses, identifying key proteins that orchestrate infection and release their genome. The study revealed three environmental conditions that induce stargate opening, allowing researchers to mimic stages of infection with high frequency.
Researchers from OIST create cheaper and user-friendly cryo-electron microscope to visualize biomolecules. The microscope uses low-energy electrons, which scatter more with lighter elements, providing a new way to image specimens.
Researchers have visualized the atomic structure of the metabolic enzyme transhydrogenase (NNT) using cryo-electron microscopy. The study reveals the enzyme's channel gating mechanism and has implications for understanding metabolic regulation and developing novel therapies.
Frankfurt researchers successfully decrypted all stages of the transport mechanism of ABC transporters, a crucial protein complex responsible for resistance to antibiotics and chemotherapy. The team used cryo-electron microscopy to obtain high-resolution images of the transporter in motion.
The new Pacific Northwest Center for Cryo-EM will provide state-of-the-art technology and training to researchers nationwide. The facility will enable scientists to see molecules in breathtaking detail, with resolution near atomic levels, revolutionizing the understanding of disease at the molecular level.
UCLA biochemists have developed a new technique called cryo-electron microscopy that allows them to view large biomolecules like viruses in extraordinary detail. Using this method, they have successfully imaged the smallest protein ever seen by this technique, paving the way for better understanding of disease-causing proteins.
Researchers at MSU have discovered a new way viruses assemble themselves and eject DNA into host cells, with potential applications in medicine and biotechnology. The study focused on the Acidianus tailed spindle virus, which can change shape to interact with its host cells.
A research team has discovered a critical moment when DNA escapes from the mitochondria during cell death, potentially triggering autoimmune diseases. This 'Great Escape' moment may one day prove crucial for understanding inflammatory and autoimmune conditions.
New research reveals heterochromatin is less dense than previously thought and features a velcro-like protein called HP1 that allows genes to be locked down. The study's findings have implications for understanding higher-order structures like nucleosome strings.
The 2017 Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for developing cryo-electron microscopy. This technology allows researchers to freeze biomolecules mid-movement and define protein structures at atomic resolution.
A team of researchers has determined the structure of an amyloid fibril with unprecedented resolution, revealing new details on its growth and effect of genetic risk factors. The atomic-level three-dimensional structure displays how Aβ protein molecules are staggered in layers to form protofilaments.
Researchers have provided high-resolution insights into the light harvesting process of plants under low light conditions. The study reveals the structural features and energy transfer pathways within the C2S2M2-type PSII-LHCII supercomplex, shedding light on its functional regulation and oxygen-evolving activity.
A new tilted microscopy technique reveals better protein structures, resolving missing information and improving disease research. This approach could lead to a deeper understanding of proteins' conformations and their role in various diseases.
Researchers captured the first cryo-electron microscopy snapshots of a key cellular receptor in action, providing near-atomic-resolution images. The study reveals how peptide hormones like GLP-1 bind to and transmit signals through G protein-coupled receptors.
A team of MSU scientists mapped a giant Samba virus using DIY cryo-electron microscopy technology, revealing its structure and biological mechanisms. The breakthrough could lead to new treatments for diseases caused by similar viruses.
Researchers localized and visualized hydrogen in steels and alloys at atomic resolution, overcoming a major engineering challenge. This discovery enables the development of new alloys with greater endurance.
The discovery of the human aichi virus atomic structure is crucial for understanding its entry into host cells and evolution. The research reveals unique structural features, including a polyproline helix that acts as a recognition motif for binding to the enteric receptor.
A recent study by Duke-NUS Medical School scientists has revealed the Zika virus structure and identified potential sites to target with therapeutics. The findings suggest that destabilizing the virus's structure may help reduce disease severity or limit transmission.
Scientists at Berkeley Lab have developed MIDI-STEM, a new method that improves images of light elements using fewer electrons. This technique allows for high-resolution views of lightweight atoms and materials with a mixture of heavy and light elements.
Researchers at Scripps Research Institute reveal the three-dimensional structure of TRPV2 ion channel, shedding light on its role in detecting infection and inflammation. The study's findings pave the way for developing new therapies to treat autoimmune diseases.
Researchers have developed a new method to display the spatial structure of nuclear pores in high resolution. This has led to a better understanding of how certain molecules are transported into or out of the nucleus. The discovery sheds light on various diseases, including cancer, that involve defective transport through nuclear pores.
Scientists have developed a new technique that allows them to create detailed 3D images of individual proteins using cryo-electron microscopy. This breakthrough enables researchers to study the flexibility and movement of proteins, which is crucial for understanding their function and developing new drugs.
Researchers at UCLA have imaged a virus structure at an atomic resolution of 3.3 angstroms using cryo-electron microscopy, allowing them to study the virus's functionality in its native environment. This breakthrough demonstrates the potential of Cryo-EM for producing high-resolution images of biological samples.
Researchers from Imperial College London and CNRS-Inserm-Strasbourg University have developed a technique to capture the protein-making factory, or ribosome, in action using cryo-electron microscopy. This will help scientists understand how many antibiotics interfere with the final steps of protein synthesis.
The new cryo-electron microscope allows for unprecedented high-resolution imaging of individual molecules and cellular structures, enabling scientists to study complex diseases such as diabetes, obesity, and Alzheimer's disease