Articles tagged with Cryo Electron Microscopy
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Scientists have identified a previously unknown molecular mechanism for initiating gene transcription in cells under stress. Using cryogenic electron microscopy, they observed how dinucleoside polyphosphate molecules bind to RNA polymerase, enabling the formation of alternative caps that protect cellular RNA.
The newly inaugurated cryo plasma-FIB scanning electron microscope with nanomanipulator at Goethe University Frankfurt enables imaging of living cells and provides new insights into cellular structures. Researchers can now visualize protein structures in their natural environment or trace cellular changes in diseases.
Researchers at Harvard Medical School have uncovered crucial insights into how a new class of antiviral drugs works, shedding light on an important tool for fighting drug-resistant strains of herpes simplex virus. The discovery may lead to new pathways for treating herpesviruses and other kinds of DNA viruses.
Researchers at Lund University have discovered a cell's protective mechanism against excessive hydrogen peroxide, a key free radical. The study shows that the channel in the cell membrane closes automatically when high concentrations of hydrogen peroxide are detected, preventing damage and cell death.
A team of researchers has captured the process of synaptic vesicle fusion with neurotransmitters, revealing a direct form of vesicle recruitment that enables neurons to send signals over longer periods. This breakthrough could lead to targeted therapies for synaptic disorders and improve our understanding of brain function.
Intellicule will utilize state-of-the-art deep-learning techniques to expand structural modeling and analysis for cryo-EM data. The company aims to overcome current limitations in biomolecular modeling, enabling the detection of atoms in low-resolution images.
Researchers at MBL propose a model for how properties of individual molecules emerge to form liquid droplets called condensates. By combining imaging and computer simulations, they reveal the importance of linker DNA in determining condensate structure.
Scientists capture unprecedented detail of a large RNA molecule assembling itself into a functional machine, overcoming kinetic traps. The research reveals the dynamic process, including subtle movements that prompt each domain to enter at precisely the right moment.
Researchers have mapped the full structure of bacteriophage Bas63 using cryo-EM, revealing unique decoration proteins and a rare whisker and collar structure. The detailed structural information will enable rational phage design and engineering efforts for specificity and target regions.
Researchers have captured a key part of the ribosome formation process, revealing how cells coordinate, regulate, and safeguard protein factory creation. The 'molecular movie' shows the role of Mtr4 enzyme and Utp14 protein in assembly, as well as an elaborate system of built-in safeguards.
Researchers have unraveled the structure of two key malaria parasite proteins, offering opportunities for new vaccines that block mosquito transmission. The discovery is a significant step towards eradicating the deadly disease.
Researchers have developed a liquid helium-cooled sample holder that allows scientists to maintain specimen temperatures as low as -423 degrees Fahrenheit for over 10 hours. This enables the study of how materials acquire properties useful in quantum computers, such as superconductivity and quantum computing capabilities.
Five University of Groningen scientists receive €1.5 million ERC Starting Grants to study brain waves and memory, develop robots with a sense of touch, create ultra-hard coatings for extreme conditions, simulate exoplanet evolution, and explore actin-based motility of human pathogens
Researchers mapped the surface envelope glycoprotein of human endogenous retroviruses, opening doors to new diagnostic and therapeutic opportunities. The study revealed specific antibodies that target the viral proteins, potentially leading to new cancer immunotherapies and treatments for autoimmune diseases.
Scientists at the Max Planck Institute for the Science of Light developed a new method to resolve specific sites within mechanosensitive protein PIEZO1 in its native cell membrane state. The technique, using cryogenic conditions and rapid freezing, sheds light on how the protein flexes and expands in response to mechanical stimuli.
A team of researchers has established the first comprehensive model of how calcium is transported out of the cell by the plasma membrane Ca²⁺-ATPase, explaining its high speed. The model reveals that PIP₂ stabilizes calcium binding and facilitates rapid release, making it the pump's primary acceleration factor.
A new imaging method, combining cryo-TEM and EELS, allows for simultaneous visualization of structure and elemental distribution in nanomaterials. The technique has been successfully applied to organic nano-materials and biomaterials like hydroxyapatite particles.
Scientists have found that nucleosomes act as gatekeepers for p53's molecular partners, controlling its access to the genetic code. This discovery reveals a new layer of regulation over p53's activity and opens possibilities for developing cancer therapies that restore or control p53 function.
The study reveals that four units of ZapA protein form an asymmetric ladder-like structure with FtsZ protofilaments, impacting the alignment of the Z-ring. The interaction between ZapA and FtsZ is dynamic, with cooperative binding and structural alterations, enabling the maintenance of FtsZ mobility.
Researchers developed a novel Cu-Al-Mn alloy with a special shape memory effect at temperatures as low as -200°C, surpassing previous limitations. The alloy's potential applications include high-performance actuators for cooling systems in space telescopes and advanced carbon-neutral initiatives.
The team built a high-resolution 3D structure of the Powassan virus, shedding light on its transmission and potential therapeutics. The findings could inform future treatments and preventions for this emerging tick-borne disease.
Biophysicist Christian Spahn's ERC Advanced Grant project aims to capture the ultra-fast intermediate steps of ribosomes in action. Using a supermicroscope, his team will analyze hundreds of thousands of images to visualize rare, short-lived states of ribosomes at atomic resolution.
Researchers achieved direct measurement of nanometer-scale charge distributions formed at ferroelectric domain interfaces using electron microscopy. This study contributes to a deeper understanding of ferroelectric devices and their performance improvement.
Researchers used cryo-electron microscopy to visualize the 3D structure of sulfite reductase, a protein enzyme that breaks down sulfur into hydrogen sulfide. This breakthrough allows scientists to better understand how the enzyme functions and its potential applications in industries such as drug manufacturing.
A new method called MagIC cryo-EM dramatically improves imaging capabilities by reducing sample loss, enabling the visualization of rare proteins and viruses. The technology also addresses the challenge of handling small proteins, allowing for more accurate structural analysis.
Tadashi Isa returns to NIPS as director with goal to foster young researchers and maintain balance between cutting-edge research and collaborative studies. He aims to elevate physiological and neuroscience research in Japan to a world-class level.
Scientists have captured the first detailed molecular movie of DNA being unzipped at the atomic level, revealing how cells copy their genetic material. The discovery has significant implications for understanding viral and cancer replication.
A team of scientists used cryo-electron microscopy to investigate G-quadruplexes, which have gained attention as potential therapeutic targets in cancer. The study reveals how secondary DNA structures like G4s can impede DNA replication and provides new insights into fundamental human biology.
Scientists have uncovered the molecular structure of Mycoplasma mobile's twin motors that power its gliding ability, using cryo-electron microscopy. The complex structure reveals a new mechanism by which energy from ATP hydrolysis is converted into motility.
Researchers used cryo-electron microscopy to determine the atomic structure of collagen assemblies with an unexpected right-handed superhelical twist. This discovery could reshape biomedical research by revealing greater structural diversity in collagen.
ApoB100 protein structure revealed for the first time, allowing for more precise testing and treatment of high cholesterol and heart disease. The discovery may lead to new drugs targeting LDL particles, reducing side effects of statin drugs.
The Department of Energy's new research centers, led by SLAC National Accelerator Laboratory, aim to make microelectronics more energy efficient and operate in extreme environments. Researchers will focus on innovating material design, devices, and systems architectures to push computing and sensing capabilities.
Researchers use cryo-electron microscopy to study Microprocessor's interactions with primary microRNAs. The protein can process multiple pri-miRNAs due to its flexibility and 'tentacle-like' properties.
Scientists have captured 3D snapshots of individual RNA nanoparticles in motion, showcasing the dynamic and intricate folding process. This breakthrough uses advanced electron microscopy to study RNA's flexibility, enabling new insights into its structure and potential applications in molecular medicine.
Researchers at IOCB Prague have discovered the HelD protein's role in protecting bacterial RNA polymerase from antibiotic effects. The protein not only frees the enzyme but also ensures its recycling, allowing bacteria to multiply again.
Osaka Metropolitan University researchers developed a new approach to analyze the 3D structure of lab-made photosynthetic antenna protein complex LHCII. Their findings validated natural antenna mimicry in artificial photosynthesis, showing only minor differences between lab-created and natural LHCII.
Researchers have identified the first high-resolution experimentally determined structure in proteins that helps bacteria survive harsh conditions. SpoIVFB, a specialized enzyme, plays a critical role in sporulation and facilitating biochemical product creation.
Researchers have gained new insights into the interaction between membrane proteins Vipp1 and PspA and their role in protecting vital cellular processes. The study reveals that these proteins form carpet-like structures, ring complexes, and tubes to stabilize and repair damaged cell membranes.
Researchers at IOCB Prague successfully isolated the proteasome enzyme complex of the T. vaginalis parasite, enabling them to develop new medicines that can target this parasite without harming humans. This breakthrough has critical implications for treating trichomoniasis and reducing HIV risk.
Researchers at the University of Münster deciphered the structure of α-latrotoxin, a potent neurotoxin that interferes with nervous system transmission. The toxin forms calcium-permeable membrane pores, inducing muscle contractions and spasms.
Researchers at ISTA have decoded the structure of HTLV-1 using Cryo-Electron Tomography, revealing a distinct viral lattice that differs from other retroviruses. This discovery could pave the way for novel treatment approaches to combat HTLV-1 infections, which affect 5-10 million people worldwide.
Researchers at Martin-Luther-Universität Halle-Wittenberg have observed proteins restructuring themselves to produce inositol, a key substance for metabolism. The study reveals that this process occurs in multiple similar proteins, shedding light on their functions.
ISTA's Lisa Bugnet, Alicia Michael, and Marco Mondelli have been awarded ERC Starting Grants to develop new methods for extracting information from data, studying gene regulation, and understanding time-keeping in cells. Their projects aim to simplify data analysis, accelerate personalized medicine, and uncover the secrets of biologica...
Researchers from IOCB Prague uncover the mechanism behind a unique termite defense, where worker termites sacrifice themselves to kill attackers. The discovery sheds light on the enzyme's durability and functionality in harsh conditions.
Researchers have used cryo-electron microscopy to reveal the structural basis of how cells regulate ferritin, a protein that stores iron. This understanding could lead to the development of drugs that block ferritin's interaction with NCOA4, slowing down aggressive cancer cells.
Researchers have visualized a molecular complex that loads a 'clamp' onto DNA to ensure accurate replication. This discovery sheds light on the intricate mechanisms of DNA replication and could improve understanding of related health conditions.
Researchers have identified the critical step in NMDAR's routine where it rotates into an open formation, enabling electrical signals crucial for cognitive functions. This discovery may pave the way for drug compounds that can correct faulty NMDARs, potentially treating conditions like Alzheimer's and depression.
Researchers at UNIGE have discovered how yeast cells respond to physical stress on their membranes. Cryo-electron microscopy revealed that specific lipid domains can stabilize and trigger cellular responses to mechanical stimuli. This study sheds light on the role of membrane compartmentalization in cell survival.
Researchers have discovered how a neutralizing antibody blocks measles virus infection by arresting the fusion process. The study's findings may also be relevant to other viruses with pandemic potential, such as Nipah and parainfluenza viruses.
Researchers used advanced imaging technology to reveal the atomic structure of an enzyme that neurons use to communicate. The study provides new insights into synaptic function and may lead to therapeutic targets for epilepsy and other neurological conditions.
Researchers identified a complex of two proteins called Gabija that enhances the blockage of phage replication in bacteria. The study found that one protein alone can disable a phage's DNA, but the complex formed with its partner protein is more effective at preventing phage takeover.
A study published in PNAS reveals the structure of a protein linked to neurodegenerative disease Niemann-Pick type C, which accumulates cholesterol within cellular compartments. The research sheds light on the complex mechanism of cholesterol distribution and its role in maintaining optimal levels.
Researchers at ISTA have discovered the composition of poxviral cores, a key factor in their infectivity. The study's findings could lead to the development of new therapeutics targeting the viral core.
Researchers have identified and detailed the structure of Mcf1, a bacterial toxin that kills insects by disrupting essential proteins in their cells. The discovery has implications for developing new organic pest control agents and may also shed light on human diseases.
Research reveals that a small subset of bacterial cells produces deadly toxins while sacrificing themselves for the benefit of their comrades. The bacteria use a temperature-sensitive genetic switch to synchronize toxin production with cell enlargement, ensuring an efficient strategy for infection.
Researchers have solved the molecular structure of a complete tailed virus with a flexible tail at unprecedented detail. This discovery has significant implications for phage therapies and the development of alternative treatments to antibiotics.
Researchers at Johannes Gutenberg University Mainz discovered a unique cryptochrome protein in marine bristle worms that distinguishes between sunlight and moonlight. The protein's structure reveals an unusual light-induced change from dimer to monomer arrangements, allowing it to synchronize reproduction with lunar phases.
Researchers at Max Planck Institute of Molecular Physiology developed an innovative imaging technique to visualize the cardiac thick filament in its native environment. The resulting high-resolution image reveals new insights into the molecular organization and function of the sarcomere, a crucial component of heart muscle contraction.
Researchers used cryo-electron microscopy to capture detailed images of key receptors, unveiling their interactions with molecules and signaling mechanisms. This study provides significant insights into a crucial receptor family within the immune system, potentially paving the way for innovative treatments.
The discovery sheds light on the mechanism of phosphate release from actin filaments, which is crucial for cell movement and disassembly. The researchers found that phosphate escapes through a molecular backdoor in the filament core, but the door remains closed for most of the time.