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A Colorized structure of a prototype for a universal flu vaccine, known as H1ssF_3928, which is being evaluated as part of a Phase 1 clinical trial at the NIH Clinical Center in Bethesda, MD. The vaccine nanoparticle, designed by Jeffrey Boyington (VRC), is a hybrid of a protein scaffold (blue) and eight influenza hemagglutinin proteins arrayed on the surface (yellow). The hemagglutinin protein was specifically engineered to display antibody binding sites common to all human influenza subtypes. The 3D structure of the particle was determined by cryo-electron microscopy by John Gallagher and Audray Harris (Laboratory of Infectious Diseases). Credit: NIAID
This image shows a cryo-electron microscopy reconstruction of the bacteriophage Phi-6 procapsid (protein shell) cut open to show the four different types of protein: blue, the P1 protein, forms the main shell; red, the P4 protein, is a hexamer NTPase that packages the single-stranded RNA genome into the shell; yellow, the P7 protein, is an essential aid for packaging; purple, the P2 protein, is the RNA-dependent RNA polymerase responsible for replication and transcription. Bacteriophage is a virus that infects bacteria. This bacteriophage is a model system for human pathogens like rotavirus that cause more than half a million deaths every year in children. Understanding the different stages in virus formation and how it packs its genetic material within the capsid may aid in developing therapeutics against the virus.
Photographer: Daniel Nemecek, Bernard Heymann, Jian Qiao, Leonard Mindich, NIAMS Laboratory of Structural Biology, Alasdair Steven, Ph.D., Chief
This image shows the RNA-packaged procapsid (protein shell) of the cystovirus, the double-stranded RNA bacteriophage Phi-6, that is used as a model system for the assembly and packaging of viruses of the eukaryotes such as the Reoviridae. Bacteriophage is a virus that infects bacteria. The data were collected by cryo-electron microscopy and the 3D structure reconstructed by computational image processing. The electron density has been rendered as a surface and colored according to the radial distance from the center of the procapsid. The inner and less ordered layers of RNA are depicted in red, the outer RNA layers that follow the structure of the outermost protein shell are colored orange and yellow, and the protein shell is shown in green and blue colors. The dark blue turrets above the 5-fold vertices are the viral RNA-packaging NTPase motors. The 2D projection under the 3D reconstruction reveals channels in the protein shell that are covered by the motors. This bacteriophage is a model system for human pathogens like rotavirus that cause more than half a million deaths every year in children. Understanding the different stages in virus formation and how it packs its genetic material within the capsid may aid in developing therapeutics against the virus.
Photographer: Daniel Nemecek, NIAMS Laboratory of Structural Biology, Alasdair Steven, Ph.D., Chief
My work instrument, the cryoelectron microscope at Vanderbilt University. Tecnai F30 (300 kV, FEG). Polara.
Coxiella burnetii-infected Vero cells (a) and Francisella tularensis-infected mouse macrophages (b) after chemical fixation, plunge freezing, fracturing, and viewing by cryo-SEM. Credit: NIAID
Bal-tec BAF 060 freeze fracture device Carbon/platinum replica of high pressure frozen and cryo-fractured yeast (a-e) and Bacillus subtilis (f-g) visualized by transmission electron microscopy. Credit: NIAID
Cryo-sections of HeLa cells infected for 20 hours with Chlamydia trachomatis. (Left) Light micrograph of frozen section cut at 300 nm. (Middle) Light micrograph of 300 nm thick section stained with anti-chlamydial and fluorescent antibodies. (Right) Transmission electron micrograph of 50 nm frozen-hydrated thin sections labeled with anti-chlamydial & 10 nm gold antibodies.
Intracellular spatial information of HeLa cell and chlamydial interactions (Fig. a, b); bacterial inclusion (Fig. c); Chlamydia revealing spike-like structures consistent with secretion apparatus (Fig. d) after chemical fixation, plunge freezing, fracturing, and viewing by cryo-SEM. Credit: NIAID
Ivan "Vanya" Zheludev presents work on September 28 of Cryo-electron Microscopy and Exploratory Antisense Targeting of the 28-kDa Frameshift Stimulation Element from the SARS-Cov-2 RNA Genome at the 2020 Virtural SSRL/LCLS Users' Meeting. (Jacqueline Orrell/SLAC National Accelerator Laboratory)
Rhiju Das and Ivan "Vanya" Zheludev present their work on September 28 of Cryo-electron Microscopy and Exploratory Antisense Targeting of the 28-kDa Frameshift Stimulation Element from the SARS-Cov-2 RNA Genome at the 2020 Virtural SSRL/LCLS Users' Meeting. (Jacqueline Orrell/SLAC National Accelerator Laboratory)
Ivan "Vanya" Zheludev presents work on September 28 of Cryo-electron Microscopy and Exploratory Antisense Targeting of the 28-kDa Frameshift Stimulation Element from the SARS-Cov-2 RNA Genome at the 2020 Virtural SSRL/LCLS Users' Meeting. (Jacqueline Orrell/SLAC National Accelerator Laboratory)
Huge discovery could change phones forever
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#CryoElectronMicroscopy, #DepartmentOfEnergySSLAC, #IPhoneOrAndroidDevice, #MaterialsAndEnergySciences, #NationalAcceleratorLaboratory, #StanfordSchoolOfMedicine
Huge discovery could change phones forever
Huge discovery could change phones forever:- Scientists have just figured out why phones don’t last as long as they could, which could pave the way for longer lasting batteries.
If you’re frustrated by how short the battery life is on your iPhone...
Researchers may have found what causes smartphone batteries to explode
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#AnotherNote7Incident, #CryoElectronMicroscopy, #ExcessElectricalChargePasses, #LithiumIonBatteries, #SamsungSGalaxyNote7Phablets
Researchers may have found what causes smartphone batteries to explode
Researchers may have found what causes smartphone batteries to explode:- Batteries have been a major concern of smartphone makers for years now, but research into better batteries took on a more urgent tone in 2016, when...