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  1. Book ; Online ; Thesis: Magnetic-force microscopy and micromagnetic simulations on domains of structured ferromagnets

    Barthelmeß, Miriam

    2004  

    Author's details vorgelegt von Miriam Barthelmeß
    Keywords Ferromagnetikum ; Rasterkraftmikroskopie ; Domänenstruktur
    Language English
    Size Online-Ressource (90 S. = 5 532,3 KB), Ill., graph. Darst.
    Publisher Staats- und Universitätsbibliothek Carl von Ossietzky
    Publishing place Hamburg
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--Hamburg, 2004
    Note Erscheinungsjahr auf d. Haupttitels.: 2003
    Database Former special subject collection: coastal and deep sea fishing

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  2. Book ; Online ; Thesis: Magnetic-force microscopy and micromagnetic simulations on domains of structured ferromagnets

    Barthelmeß, Miriam

    2004  

    Author's details vorgelegt von Miriam Barthelmeß
    Keywords Ferromagnetikum ; Rasterkraftmikroskopie ; Domänenstruktur
    Language English
    Size Online-Ressource (90 S. = 5 532,3 KB), Ill., graph. Darst.
    Publisher Staats- und Universitätsbibliothek Carl von Ossietzky
    Publishing place Hamburg
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--Hamburg, 2004
    Note Erscheinungsjahr auf d. Haupttitels.: 2003
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  3. Article: Fixed-target serial femtosecond crystallography using

    Lahey-Rudolph, J Mia / Schönherr, Robert / Barthelmess, Miriam / Fischer, Pontus / Seuring, Carolin / Wagner, Armin / Meents, Alke / Redecke, Lars

    IUCrJ

    2021  Volume 8, Issue Pt 4, Page(s) 665–677

    Abstract: The crystallization of recombinant proteins in living cells is an exciting new approach in structural biology. Recent success has highlighted the need for fast and efficient diffraction data collection, optimally directly exposing intact crystal- ... ...

    Abstract The crystallization of recombinant proteins in living cells is an exciting new approach in structural biology. Recent success has highlighted the need for fast and efficient diffraction data collection, optimally directly exposing intact crystal-containing cells to the X-ray beam, thus protecting the
    Language English
    Publishing date 2021-06-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2754953-7
    ISSN 2052-2525
    ISSN 2052-2525
    DOI 10.1107/S2052252521005297
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Thermal and stress studies of normal incidence Mo/B4C multilayers for a 6.7 nm wavelength.

    Barthelmess, Miriam / Bajt, Saša

    Applied optics

    2011  Volume 50, Issue 11, Page(s) 1610–1619

    Abstract: Wavelength, reflectance, and stress stability of Mo/B(4)C multilayers were studied as a function of postdeposition annealing up to 900 °C. These multilayers are of interest as normal incidence coatings for wavelengths above the boron K-absorption edge. ... ...

    Abstract Wavelength, reflectance, and stress stability of Mo/B(4)C multilayers were studied as a function of postdeposition annealing up to 900 °C. These multilayers are of interest as normal incidence coatings for wavelengths above the boron K-absorption edge. Mo/B(4)C multilayers deposited at low sputtering pressure have high compressive stress. Zero stress can be achieved at 360 °C-370 °C, but annealing at <200 °C is sufficient to reduce stress by ∼40%. This stress relaxation is accompanied with a multilayer period expansion of ∼0.02 nm and a <0.5% decrease in normal incidence reflectivity. The multilayer period remains stable up to ∼600 °C, while intrinsic stress changes from compressive to tensile. A four-layer model with amorphous molybdenum and boron carbide layers separated by amorphous layers of molybdenum borides (Mo(x)B(y)) is presented. These interlayers are present already in the as-deposited state and continue to grow with increasing temperature. Their presence lowers the optical contrast and the achievable reflectivity. However, they also increase multilayer thermal stability. At temperatures >600 °C, a noticeable decrease in reflectivity associated with the phase transition from amorphous to crystalline molybdenum boride is observed. This is accompanied with an increase in interface and surface roughness and a change in stress as a function of temperature.
    Language English
    Publishing date 2011-04-10
    Publishing country United States
    Document type Journal Article
    ISSN 1539-4522
    ISSN (online) 1539-4522
    DOI 10.1364/AO.50.001610
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Book ; Thesis: Magnetic-force microscopy and micromagnetic simulations on domains of structured ferromagnets

    Barthelmeß, Miriam

    2003  

    Author's details vorgelegt von Miriam Barthelmeß, geb. Halverscheid
    Keywords Ferromagnetikum ; Rasterkraftmikroskopie ; Domänenstruktur
    Language English
    Size 83 S, Ill., graph. Darst
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Univ., FB Physik, Diss.--Hamburg, 2004
    Note Enth. Zeitschriftensonderabdrucke ; Zsfassung in dt. Sprache
    Database Former special subject collection: coastal and deep sea fishing

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  6. Article ; Online: Multimodal X-ray imaging of nanocontainer-treated macrophages and calcium distribution in the perilacunar bone matrix.

    Stachnik, Karolina / Warmer, Martin / Mohacsi, Istvan / Hennicke, Vincent / Fischer, Pontus / Meyer, Jan / Spitzbart, Tobias / Barthelmess, Miriam / Eich, Jacqueline / David, Christian / Feldmann, Claus / Busse, Björn / Jähn, Katharina / Schaible, Ulrich E / Meents, Alke

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 1784

    Abstract: Studies of biological systems typically require the application of several complementary methods able to yield statistically-relevant results at a unique level of sensitivity. Combined X-ray fluorescence and ptychography offer excellent elemental and ... ...

    Abstract Studies of biological systems typically require the application of several complementary methods able to yield statistically-relevant results at a unique level of sensitivity. Combined X-ray fluorescence and ptychography offer excellent elemental and structural imaging contrasts at the nanoscale. They enable a robust correlation of elemental distributions with respect to the cellular morphology. Here we extend the applicability of the two modalities to higher X-ray excitation energies, permitting iron mapping. Using a long-range scanning setup, we applied the method to two vital biomedical cases. We quantified the iron distributions in a population of macrophages treated with Mycobacterium-tuberculosis-targeting iron-oxide nanocontainers. Our work allowed to visualize the internalization of the nanocontainer agglomerates in the cytosol. From the iron areal mass maps, we obtained a distribution of antibiotic load per agglomerate and an average areal concentration of nanocontainers in the agglomerates. In the second application we mapped the calcium content in a human bone matrix in close proximity to osteocyte lacunae (perilacunar matrix). A concurrently acquired ptychographic image was used to remove the mass-thickness effect from the raw calcium map. The resulting ptychography-enhanced calcium distribution allowed then to observe a locally lower degree of mineralization of the perilacunar matrix.
    MeSH term(s) Animals ; Bone Matrix/diagnostic imaging ; Bone Matrix/metabolism ; Bone Remodeling/physiology ; Calcium/metabolism ; Macrophages/metabolism ; Mice ; Multimodal Imaging/methods ; X-Rays
    Chemical Substances Calcium (SY7Q814VUP)
    Language English
    Publishing date 2020-02-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-58318-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Imaging via Correlation of X-Ray Fluorescence Photons.

    Trost, Fabian / Ayyer, Kartik / Prasciolu, Mauro / Fleckenstein, Holger / Barthelmess, Miriam / Yefanov, Oleksandr / Dresselhaus, J Lukas / Li, Chufeng / Bajt, Saša / Carnis, Jerome / Wollweber, Tamme / Mall, Abhishek / Shen, Zhou / Zhuang, Yulong / Richter, Stefan / Karl, Sebastian / Cardoch, Sebastian / Patra, Kajwal Kumar / Möller, Johannes /
    Zozulya, Alexey / Shayduk, Roman / Lu, Wei / Brauße, Felix / Friedrich, Bertram / Boesenberg, Ulrike / Petrov, Ilia / Tomin, Sergey / Guetg, Marc / Madsen, Anders / Timneanu, Nicusor / Caleman, Carl / Röhlsberger, Ralf / von Zanthier, Joachim / Chapman, Henry N

    Physical review letters

    2023  Volume 130, Issue 17, Page(s) 173201

    Abstract: We demonstrate that x-ray fluorescence emission, which cannot maintain a stationary interference pattern, can be used to obtain images of structures by recording photon-photon correlations in the manner of the stellar intensity interferometry of Hanbury ... ...

    Abstract We demonstrate that x-ray fluorescence emission, which cannot maintain a stationary interference pattern, can be used to obtain images of structures by recording photon-photon correlations in the manner of the stellar intensity interferometry of Hanbury Brown and Twiss. This is achieved utilizing femtosecond-duration pulses of a hard x-ray free-electron laser to generate the emission in exposures comparable to the coherence time of the fluorescence. Iterative phasing of the photon correlation map generated a model-free real-space image of the structure of the emitters. Since fluorescence can dominate coherent scattering, this may enable imaging uncrystallised macromolecules.
    Language English
    Publishing date 2023-05-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 208853-8
    ISSN 1079-7114 ; 0031-9007
    ISSN (online) 1079-7114
    ISSN 0031-9007
    DOI 10.1103/PhysRevLett.130.173201
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: On-chip crystallization for serial crystallography experiments and on-chip ligand-binding studies.

    Lieske, Julia / Cerv, Maximilian / Kreida, Stefan / Komadina, Dana / Fischer, Janine / Barthelmess, Miriam / Fischer, Pontus / Pakendorf, Tim / Yefanov, Oleksandr / Mariani, Valerio / Seine, Thomas / Ross, Breyan H / Crosas, Eva / Lorbeer, Olga / Burkhardt, Anja / Lane, Thomas J / Guenther, Sebastian / Bergtholdt, Julian / Schoen, Silvan /
    Törnroth-Horsefield, Susanna / Chapman, Henry N / Meents, Alke

    IUCrJ

    2019  Volume 6, Issue Pt 4, Page(s) 714–728

    Abstract: Efficient and reliable sample delivery has remained one of the bottlenecks for serial crystallography experiments. Compared with other methods, fixed-target sample delivery offers the advantage of significantly reduced sample consumption and shorter data ...

    Abstract Efficient and reliable sample delivery has remained one of the bottlenecks for serial crystallography experiments. Compared with other methods, fixed-target sample delivery offers the advantage of significantly reduced sample consumption and shorter data collection times owing to higher hit rates. Here, a new method of on-chip crystallization is reported which allows the efficient and reproducible growth of large numbers of protein crystals directly on micro-patterned silicon chips for
    Language English
    Publishing date 2019-06-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 2754953-7
    ISSN 2052-2525
    ISSN 2052-2525
    DOI 10.1107/S2052252519007395
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: High numerical aperture multilayer Laue lenses.

    Morgan, Andrew J / Prasciolu, Mauro / Andrejczuk, Andrzej / Krzywinski, Jacek / Meents, Alke / Pennicard, David / Graafsma, Heinz / Barty, Anton / Bean, Richard J / Barthelmess, Miriam / Oberthuer, Dominik / Yefanov, Oleksandr / Aquila, Andrew / Chapman, Henry N / Bajt, Saša

    Scientific reports

    2015  Volume 5, Page(s) 9892

    Abstract: The ever-increasing brightness of synchrotron radiation sources demands improved X-ray optics to utilise their capability for imaging and probing biological cells, nanodevices, and functional matter on the nanometer scale with chemical sensitivity. Here ... ...

    Abstract The ever-increasing brightness of synchrotron radiation sources demands improved X-ray optics to utilise their capability for imaging and probing biological cells, nanodevices, and functional matter on the nanometer scale with chemical sensitivity. Here we demonstrate focusing a hard X-ray beam to an 8 nm focus using a volume zone plate (also referred to as a wedged multilayer Laue lens). This lens was constructed using a new deposition technique that enabled the independent control of the angle and thickness of diffracting layers to microradian and nanometer precision, respectively. This ensured that the Bragg condition is satisfied at each point along the lens, leading to a high numerical aperture that is limited only by its extent. We developed a phase-shifting interferometric method based on ptychography to characterise the lens focus. The precision of the fabrication and characterisation demonstrated here provides the path to efficient X-ray optics for imaging at 1 nm resolution.
    Language English
    Publishing date 2015-06-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep09892
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Conformation sequence recovery of a non-periodic object from a diffraction-before-destruction experiment.

    Yoon, Chun Hong / Barthelmess, Miriam / Bean, Richard J / Capotondi, Flavio / Kirian, Richard A / Kiskinova, Maya / Pedersoli, Emanuele / Raimondi, Lorenzo / Stellato, Francesco / Wang, Fenglin / Chapman, Henry N

    Optics express

    2014  Volume 22, Issue 7, Page(s) 8085–8093

    Abstract: Knowledge of the sequence of different conformational states of a protein molecule is key to better understanding its biological function. A diffraction pattern from a single conformational state can be captured with an ultrafast X-ray Free-Electron ... ...

    Abstract Knowledge of the sequence of different conformational states of a protein molecule is key to better understanding its biological function. A diffraction pattern from a single conformational state can be captured with an ultrafast X-ray Free-Electron Laser (XFEL) before the target is completely annihilated by the radiation. In this paper, we report the first experimental demonstration of conformation sequence recovery using diffraction patterns from randomly ordered conformations of a non-periodic object using the dimensional reduction technique Isomap and coherent diffraction imaging.
    Language English
    Publishing date 2014-04-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1491859-6
    ISSN 1094-4087 ; 1094-4087
    ISSN (online) 1094-4087
    ISSN 1094-4087
    DOI 10.1364/OE.22.008085
    Database MEDical Literature Analysis and Retrieval System OnLINE

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