Articles tagged with Cryo Electron Microscopy
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.
The study reveals a quantum switching mechanism of LHCII, which regulates energy transfer quantum channel in response to lateral pressure and conformational change. This mechanism enables high efficiency in photosynthesis and balanced photoprotection.
Researchers have discovered how plants pass along chemical markers that instruct cells on using DNA codes, a process known as epigenetic inheritance. The study reveals the role of protein DDM1 in making way for enzymes that add regulatory marks to new DNA strands, preserving genetic controls across generations.
Researchers reconstructed six states of a rotary sodium ion pump using cryo-electron microscopy. The study found non-uniform rotation behavior due to structural interference between the rotor and stator components. This reveals a unique molecular mechanism of the rotary sodium ion pump.
Scientists have developed a way to program virus particles' size and shape using DNA origami nanostructures, potentially advancing vaccine development and drug delivery. The approach uses electrostatic interactions between DNA nanostructures and capsid proteins to create user-defined assemblies.
Researchers discovered that extracellular cytochrome nanowires are widespread in prokaryotic microbes, including both bacteria and archaea. The findings suggest that these nanowires, composed of a long chain of cytochrome proteins, play a crucial role in microbial metabolism by facilitating efficient electron transfer.
The study reveals that the GABA transporter structure is facing the cytosol and bound to a GABA molecule, sodium, and chloride ions. This binding mechanism is crucial for understanding GABA recognition and release into neurons.
Scientists have gained high-res structural insights into a key bacterial enzyme to develop new drugs that target its weaknesses and suppress disease-causing bacteria. The enzyme Lnt is not found in humans and has huge potential as a therapeutic target with fewer side effects for patients.
Researchers used cryo-electron tomography to study the dynein motor protein, revealing new details about how it generates force and coordinates with other proteins. This knowledge may help develop treatments for diseases related to cilia dysfunction, such as fertility issues and lung disease.
Researchers discovered a protein complex called FERRY that plays a crucial role in transporting messenger RNA in neurons. The study provided evidence of the transport of mRNA using Early Endosomes (EEs) and a novel mode of binding RNA via coiled-coil domains.
A team at Penn State has produced high-resolution images of SARS-CoV-2's protease protein and polyprotein complex. The research reveals a consistent order in which the proteins are cleaved, potentially supporting more efficient antiviral drugs.
Researchers at IOCB Prague have determined the first cryo-EM structures of a surface receptor of Trypanosoma brucei gambiense in complex with human complement factor C3. This discovery sheds light on how the parasite avoids clearance from the human bloodstream and survives within the immune system.
Researchers have identified the structure of the circadian rhythm photosensor and its target in fruit flies, revealing key components of the circadian clocks. The study also shed light on how DNA damage is repaired in a cell and found genetic variations that help flies adapt to changing latitudes.
Researchers use cryo-electron microscopy to visualize a sirtuin enzyme bound to a nucleosome, clarifying how it accesses DNA and histone proteins to modulate gene expression. The study provides insight into the function of SIRT6 in humans and other animals.
Researchers at the University of Tokyo have discovered the 3D structure of TnpB, a protein involved in genome editing and a probable precursor to the CRISPR-Cas12 enzyme. The study reveals how TnpB recognizes and cuts DNA using a unique pseudoknot shape similar to that found in guide RNAs of Cas12 enzymes.
Researchers from PSI deciphered the structure of an ion channel found in the eye while interacting with calmodulin, a protein that enables cell response to calcium fluctuations. This interaction is believed to be responsible for achieving remarkable sensitivity to dim light.
Researchers at UC San Francisco have created the first molecular-level picture of how an odor molecule activates a human odorant receptor, opening doors to creating novel smells. This achievement paves the way for new insights into biological processes, including fragrances and food science.
Scientists at Aarhus University and Berkeley Laboratory developed a method called RNA origami to design artificial RNA nanostructures. The technique allowed for the discovery of rules and mechanisms for RNA folding that will make it possible to build more ideal RNA particles for use in RNA-based medicine.
Researchers have unveiled the structure of DREADDs, a neural tool that enables precise control over neurons. The new findings will allow for further refinement and optimization of the tool, paving the way for innovative treatments for brain disorders such as schizophrenia, substance abuse, and Alzheimer's.
Researchers create advanced imaging-based method for studying mitochondria, enabling detailed mapping and measurement of structural changes. This technique has potential applications in understanding diseases such as Alzheimer’s, Parkinson’s, and cancers where mitochondrial function is disrupted.
The São Paulo School of Advanced Science on Cryogenic Electron Microscopy will be held at the University of São Paulo from July 10-27, 2023. The event will cover theoretical and practical foundations of advanced CryoEM techniques, featuring renowned researchers and hands-on practical sessions.
Researchers at Osaka University used cryogenic electron microscopy to study the structural change of the centromere during cell division. The study revealed a complex interaction between proteins involved in cell division, providing new insights into the correct division of chromosomes.
Researchers at Universitat Autonoma de Barcelona solved the structure of a functional amyloid protein, hnRNPDL-2, which forms stable and non-toxic fibres in humans. The discovery changes the concept of disease origin and treatment, suggesting that molecules stabilising or facilitating fibre formation could be the key to therapy.
Researchers have shed new light on viral genome replication machinery, revealing its intricate structure at atomic resolution. The study, published in PNAS, provides essential insights into the assembly, dynamic operation, and potential therapeutic targets of this complex machine.
Researchers at St. Jude Children's Research Hospital used cryo-electron microscopy to capture the first 3D structure of SPOP, a protein mutated in prostate and endometrial cancers. The study revealed previously unknown interfaces that harbor cancer-causing mutations, shedding light on how SPOP drives cancer.
A potent plant toxin called albicidin has emerged as a strong new antibiotic candidate, effective in small concentrations and highly potent against pathogenic bacteria. Its unique mechanism targets the bacterial enzyme DNA gyrase, which is essential for cell function.
Researchers at Aston University have created the world's first computer reconstruction of a virus, including its complete native genome. This breakthrough could lead to the development of targeted treatments to kill bacteria that are dangerous to humans, reducing the threat of antibiotic resistance.
Researchers used high-voltage electron microscopy to image frozen tokyovirus particles in detail, revealing a novel capsid protein network and scaffold protein component. The study provides new insights into the structure and function of giant viruses, which are larger than small bacteria.
Researchers have gained a better understanding of the structures and functions of Andhra gene products, paving the way for custom phages for therapeutic applications. The high-resolution knowledge of the virus structure is crucial for developing targeted treatments against Staphylococcus epidermidis infections.
Researchers have discovered the three-dimensional structure of phosphoinositide 3-kinase alpha (PI3Kα) and how it changes with cancer-associated mutations. This knowledge enables the design of targeted drugs that can specifically bind to mutated versions, potentially eliminating side effects associated with current PI3Kα inhibitors.
Scientists have clarified the structure of a new protein complex that catalyses energy conversion processes in photosynthesis, known as Photosystem I. The research reveals that two monomers can join together as a dimer, leading to improved hydrogen production in certain plant species.
Poliovirus researchers at Umeå University have gained a new understanding of how the virus behaves in infected cells, revealing key protein roles and cellular processes involved. This breakthrough could lead to the development of new antiviral treatments and vaccines targeting the autophagy system.
Researchers used advanced imaging techniques to understand the structure of bacterial propellers, which are made of a single protein. The study reveals that bacteria push themselves forward by coiling these appendages into corkscrew shapes, and that similar structures have evolved independently in archaea.
Researchers developed a new method combining cryo-EM with iDPC-STEM, achieving sub-nanometer resolution for protein structures. This technique expands possibilities for structural analysis of heterogeneous and single-particle samples.
Researchers captured first image of antigen-bound T-cell receptor complex with bound antigen at atomic resolution. The study reveals no significant structural changes in the receptor after antigen binding, sparking further investigation into the signaling pathway activation mechanism.
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.