Thematische Bibliographien / Cryogenic electron tomography

Auswahl der wissenschaftlichen Literatur zum Thema „Cryogenic electron tomography“

Autor: Grafiati

Veröffentlicht am 25. Mai 2024

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Zeitschriftenartikel zum Thema "Cryogenic electron tomography"

Zickert, Gustav, und Simon Maretzke. „Cryogenic electron tomography reconstructions from phaseless data“. Inverse Problems 34, Nr. 12 (04.10.2018): 124001. http://dx.doi.org/10.1088/1361-6420/aade22.

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Carlson, David B., Jeff Gelb, Vadim Palshin und James E. Evans. „Laboratory-Based Cryogenic Soft X-Ray Tomography with Correlative Cryo-Light and Electron Microscopy“. Microscopy and Microanalysis 19, Nr. 1 (18.01.2013): 22–29. http://dx.doi.org/10.1017/s1431927612013827.

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AbstractHere we present a novel laboratory-based cryogenic soft X-ray microscope for whole cell tomography of frozen hydrated samples. We demonstrate the capabilities of this compact cryogenic microscope by visualizing internal subcellular structures of Saccharomyces cerevisiae cells. The microscope is shown to achieve better than 50 nm half-pitch spatial resolution with a Siemens star test sample. For whole biological cells, the microscope can image specimens up to 5 μm thick. Structures as small as 90 nm can be detected in tomographic reconstructions following a low cumulative radiation dose of only 7.2 MGy. Furthermore, the design of the specimen chamber utilizes a standard sample support that permits multimodal correlative imaging of the exact same unstained yeast cell via cryo-fluorescence light microscopy, cryo-soft X-ray microscopy, and cryo-transmission electron microscopy. This completely laboratory-based cryogenic soft X-ray microscope will enable greater access to three-dimensional ultrastructure determination of biological whole cells without chemical fixation or physical sectioning.

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Ong, Quy, Ting Mao, Neda Iranpour Anaraki, Łukasz Richter, Carla Malinverni, Xufeng Xu, Francesca Olgiati et al. „Cryogenic electron tomography to determine thermodynamic quantities for nanoparticle dispersions“. Materials Horizons 9, Nr. 1 (2022): 303–11. http://dx.doi.org/10.1039/d1mh01461g.

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Yipyintum, Chetarpa, Ji Yeong Lee, Jin-Yoo Suh und Boonrat Lohwongwatana. „Hydride formation mechanisms in Zr-containing amorphous alloys during sample preparation and atom probe tomography“. Materials Testing 65, Nr. 3 (01.03.2023): 431–37. http://dx.doi.org/10.1515/mt-2022-0452.

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Abstract Hydride formation in Zr-containing amorphous alloys as an experimental artifact was investigated utilizing atom probe tomography, transmission electron microscopy, and focused ion beam with normal and cryogenic conditions. The amount of hydrogen existing in the atom probe specimens decreased significantly by utilizing focused ion beam milling under cryogenic condition. Also, the formation of hydride was confirmed by diffraction pattern analysis in the remaining tip of the specimen after the atom probe tomography experiment. With those collected pieces of evidence, sources of hydrogen in the atom probe tomography were discussed.

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Chang, Yi-Wei, Songye Chen, Elitza I. Tocheva, Anke Treuner-Lange, Stephanie Löbach, Lotte Søgaard-Andersen und Grant J. Jensen. „Correlated cryogenic photoactivated localization microscopy and cryo-electron tomography“. Nature Methods 11, Nr. 7 (11.05.2014): 737–39. http://dx.doi.org/10.1038/nmeth.2961.

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Dahlberg, Peter D., Saumya Saurabh, Jiarui Wang, Annina M. Sartor, Wah Chiu, Lucy Shapiro und William E. Moerner. „Cryogenic Superresolution Fluorescence Correlated with Cryogenic Electron Tomography: Combining Specific Labeling and High Resolution“. Biophysical Journal 118, Nr. 3 (Februar 2020): 20a—21a. http://dx.doi.org/10.1016/j.bpj.2019.11.293.

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Frischknecht, Freddy, und Marek Cyrklaff. „Imaging Motile Pathogens with Light Microscopy and Cryogenic Electron Tomography“. Microscopy Today 17, Nr. 6 (November 2009): 30–35. http://dx.doi.org/10.1017/s1551929509991027.

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The most prominent vector-transmitted diseases in the first and third world are Lyme disease and malaria, respectively. In both cases the transmitted agents are introduced into the skin from where they eventually disseminate into the blood using active motility. We are interested in deciphering the molecular mechanisms underlying the motility of these pathogens and how they relate to the ultrastructure of the pathogens. Here we provide an overview of the microscopy techniques that we use to achieve these goals.

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Kudryashev, Mikhail, Simone Lepper, Wolfgang Baumeister, Marek Cyrklaff und Friedrich Frischknecht. „Geometric constrains for detecting short actin filaments by cryogenic electron tomography“. PMC Biophysics 3, Nr. 1 (2010): 6. http://dx.doi.org/10.1186/1757-5036-3-6.

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Yoniles, Joseph. „Time-resolved cryogenic electron tomography with mix-and-spray microfluidic devices“. Biophysical Journal 123, Nr. 3 (Februar 2024): 419a. http://dx.doi.org/10.1016/j.bpj.2023.11.2552.

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Löbling, Tina I., Johannes S. Haataja, Christopher V. Synatschke, Felix H. Schacher, Melanie Müller, Andreas Hanisch, André H. Gröschel und Axel H. E. Müller. „Hidden Structural Features of Multicompartment Micelles Revealed by Cryogenic Transmission Electron Tomography“. ACS Nano 8, Nr. 11 (17.09.2014): 11330–40. http://dx.doi.org/10.1021/nn504197y.

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Dissertationen zum Thema "Cryogenic electron tomography"

Harastani, Mohamad. „Image analysis methods development for in vitro and in situ cryo-electron tomography studies of conformational variability of biomolecular complexes : Case of nucleosome structural and dynamics studies“. Electronic Thesis or Diss., Sorbonne université, 2022. http://www.theses.fr/2022SORUS283.

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La tomographie électronique cryogénique (cryo-TE) permet de visualiser des complexes biomoléculaires in situ. Les données 3D de biomolécules produites à l'aide de cryo-ET sont bruitées, souffrent d'anisotropies spatiales et sont difficiles à analyser individuellement. Les biomolécules sont flexibles et l'analyse de leur variabilité conformationnelle est nécessaire pour comprendre leurs mécanismes fonctionnels. Les méthodes standards de traitement de données de cryo-ET moyennent plusieurs copies de biomolécules individuelles pour obtenir des structures à des résolutions plus élevées et considèrent que la variabilité conformationnelle biomoléculaire est discrète plutôt que continue en utilisant la classification. Cette thèse présente les deux premières méthodes de traitement de données cryo-ET pour l'analyse de la variabilité conformationnelle continue biomoléculaire, HEMNMA-3D et TomoFlow. HEMNMA-3D analyse des données expérimentales avec les directions de mouvement simulées par l'Analyse de Modes Normaux et permet la découverte d'une large gamme de mouvements biomoléculaires. TomoFlow extrait des mouvements à partir des données en utilisant la technique de vision par ordinateur de Flux Optique. Je montre le potentiel de ces deux méthodes sur des données cryo-ET expérimentales de variabilité conformationnelle des nucléosomes dans les cellules. Les deux méthodes montrent des résultats cohérents, faisant la lumière sur la variabilité conformationnelle des nucléosomes dans les cellules
Cryogenic electron tomography (cryo-ET) allows visualizing biomolecular complexes in situ. 3D data of biomolecules produced using cryo-ET are noisy, suffer from spacial anisotropies, and are difficult to analyze individually. Biomolecules are flexible, and analyzing their conformational variability is necessary to understand their functional mechanisms. Standard cryo-ET data processing methods average multiple copies of individual biomolecules to obtain structures at higher resolutions and consider that biomolecular conformational variability is discrete rather than continuous using the classification. This thesis presents the first two cryo-ET data processing methods for analyzing biomolecular continuous conformational variability, HEMNMA-3D and TomoFlow. HEMNMA-3D analyzes experimental data with the motion directions simulated by Normal Mode Analysis and allows the discovery of a large range of biomolecular motions. TomoFlow extracts motions from the data using the computer vision technique of Optical Flow. I show the potential of these two methods on experimental cryo-ET data of nucleosome conformational variability in cells. The two methods show coherent results, shedding light on the conformational variability of nucleosomes in cells

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Huisman, Maximiliaan. „Vision Beyond Optics: Standardization, Evaluation and Innovation for Fluorescence Microscopy in Life Sciences“. eScholarship@UMMS, 2019. https://escholarship.umassmed.edu/gsbs_diss/1017.

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Fluorescence microscopy is an essential tool in biomedical sciences that allows specific molecules to be visualized in the complex and crowded environment of cells. The continuous introduction of new imaging techniques makes microscopes more powerful and versatile, but there is more than meets the eye. In addition to develop- ing new methods, we can work towards getting the most out of existing data and technologies. By harnessing unused potential, this work aims to increase the richness, reliability, and power of fluorescence microscopy data in three key ways: through standardization, evaluation and innovation. A universal standard makes it easier to assess, compare and analyze imaging data – from the level of a single laboratory to the broader life sciences community. We propose a data-standard for fluorescence microscopy that can increase the confidence in experimental results, facilitate the exchange of data, and maximize compatibility with current and future data analysis techniques. Cutting-edge imaging technologies often rely on sophisticated hardware and multi-layered algorithms for reconstruction and analysis. Consequently, the trustworthiness of new methods can be difficult to assess. To evaluate the reliability and limitations of complex methods, quantitative analyses – such as the one present here for the 3D SPEED method – are paramount. The limited resolution of optical microscopes prevents direct observation of macro- molecules like DNA and RNA. We present a multi-color, achromatic, cryogenic fluorescence microscope that has the potential to produce multi-color images with sub-nanometer precision. This innovation would move fluorescence imaging beyond the limitations of optics and into the world of molecular resolution.

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Buchteile zum Thema "Cryogenic electron tomography"

D’Imprima, Edoardo, Herman K. H. Fung, Ievgeniia Zagoriy und Julia Mahamid. „Cryogenic Preparations of Biological Specimens for Cryo-Electron Tomography“. In Cryo-Electron Tomography, 85–114. Cham: Springer International Publishing, 2024. http://dx.doi.org/10.1007/978-3-031-51171-4_3.

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Stass, Robert, Weng M. Ng, Young Chan Kim und Juha T. Huiskonen. „Structures of enveloped virions determined by cryogenic electron microscopy and tomography“. In Advances in Virus Research, 35–71. Elsevier, 2019. http://dx.doi.org/10.1016/bs.aivir.2019.07.009.

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A. Matthay, Zachary, und Lucy Zumwinkle Kornblith. „Platelet Imaging“. In Platelets. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91736.

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The knowledge gained through imaging platelets has formed the backbone of our understanding of their biology in health and disease. Early investigators relied on conventional light microscopy with limited resolution and were primarily able to identify the presence and basic morphology of platelets. The advent of high resolution technologies, in particular, electron microscopy, accelerated our understanding of the dynamics of platelet ultrastructure dramatically. Further refinements and improvements in our ability to localize and reliably identify platelet structures have included the use of immune-labeling techniques, correlative-fluorescence light and electron microscopy, and super-resolution microscopies. More recently, the expanded development and application of intravital microscopy in animal models has enhanced our knowledge of platelet functions and thrombus formation in vivo, as these experimental systems most closely replicate native biological environments. Emerging improvements in our ability to characterize platelets at the ultrastructural and organelle levels include the use of platelet cryogenic electron tomography with quantitative, unbiased imaging analysis, and the ability to genetically label platelet features with electron dense markers for analysis by electron microscopy.

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Luisi, Ben, und Elliott Stollar. „Protein–DNA Interactions“. In Nucleic Acids in Chemistry and Biology, 522–71. The Royal Society of Chemistry, 2022. http://dx.doi.org/10.1039/9781837671328-00522.

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In this chapter we describe how our understanding of molecular recognition in protein–DNA interactions at the level of stereochemistry and structural detail has been advanced by X-ray crystallography and nuclear magnetic resonance (NMR) and now further accelerated by cryogenic electron microscopy (cryo-EM) and machine learning. These approaches are moving to address challenging questions, such as, “How is the activity of transcription factors regulated?” “How does the organisation of chromatin into modular domains occur and how might that help to define programs of transcription?” With the development of powerful tools such as electron tomography and mapping transient interactions in situ by chromatin capture methods, we are moving toward the next stage of visualising higher order macromolecular organisation in situ, in both space and in time. These and other experimental and computational approaches will enable us to follow how the information encoded in the primary sequence of the hereditary material is manifested as the complex and difficult to predict readout, namely the biological phenotype upon which evolution acts blindly.

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Han, Bing, Xiangyan Li und Yucheng Zou. „Study about Three-Dimensional Visualization of Lithium Metal Anode via Low-Dose Cryogenic Electron Microscopy Tomography“. In Recent Progress in Science and Technology Vol. 1, 20–32. B P International (a part of SCIENCEDOMAIN International), 2023. http://dx.doi.org/10.9734/bpi/rpst/v1/8879f.

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Konferenzberichte zum Thema "Cryogenic electron tomography"

Dahlberg, Peter. „Cryogenic super-resolution fluorescence correlated with cryogenic electron tomography: combining specific labelling and high resolution context“. In Single Molecule Spectroscopy and Superresolution Imaging XV, herausgegeben von Ingo Gregor, Rainer Erdmann und Felix Koberling. SPIE, 2022. http://dx.doi.org/10.1117/12.2610478.

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