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34 results on '"Rehbein, Stefan"'

3. Ion beam lithography for Fresnel zone plates in X-ray microscopy

Author

Keskinbora, Kahraman, Grévent, Corinne, Bechtel, Michael, Weigand, Markus, Goering, Eberhard, Nadzeyka, Achim, Peto, Lloyd, Rehbein, Stefan, Schneider, Gerd, Follath, Rolf, Vila-Comamala, Joan, Yan, Hanfei, and Schütz, Gisela

Subjects
Physics - Optics
Abstract

Fresnel Zone Plates (FZP) are to date very successful focusing optics for X-rays. Established methods of fabrication are rather complex and based on electron beam lithography (EBL). Here, we show that ion beam lithography (IBL) may advantageously simplify their preparation. A FZP operable from the extreme UV to the limit of the hard X-ray was prepared and tested from 450 eV to 1500 eV. The trapezoidal profile of the FZP favorably activates its 2nd order focus. The FZP with an outermost zone width of 100 nm allows the visualization of features down to 61, 31 and 21 nm in the 1st, 2nd and 3rd order focus respectively. Measured efficiencies in the 1st and 2nd order of diffraction reach the theoretical predictions.

Published
2012
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4. Quantitative Element‐Sensitive Analysis of Individual Nanoobjects

Author

Wählisch, André, primary, Unterumsberger, Rainer, additional, Hönicke, Philipp, additional, Lubeck, Janin, additional, Kayser, Yves, additional, Weser, Jan, additional, Dai, Gaoliang, additional, Hahm, Kai, additional, Weimann, Thomas, additional, Seim, Christian, additional, Rehbein, Stefan, additional, and Beckhoff, Burkhard, additional

Published
2022
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5. Volume Effects in Zone Plates

Author

Schneider, Gerd, Rehbein, Stefan, Werner, Stephan, Rhodes, William T., editor, Erko, Alexei, editor, Idir, Mourad, editor, Krist, Thomas, editor, and Michette, Alan G., editor

Published
2008
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11. Imaging organo-mineral associations of creek sediments

Author

Eusterhues, Karin, primary, Thieme, Jürgen, additional, Lühl, Lars, additional, Haidl, Andreas, additional, Heym, S. Johannes, additional, Adrianov, Konstantin, additional, Dehlinger, Aurelie, additional, Rehbein, Stefan, additional, Wilhein, Thomas, additional, Kanngießer, Birgit, additional, and Totsche, Kai Uwe, additional

Published
2020
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12. Soft X-ray nanoscale imaging using a sub-pixel resolution charge coupled device (CCD) camera

Author

Lübcke, Andrea, primary, Braenzel, Julia, additional, Dehlinger, Aurelie, additional, Schnürer, Matthias, additional, Stiel, Holger, additional, Guttmann, Peter, additional, Rehbein, Stefan, additional, Schneider, Gerd, additional, Werner, Stephan, additional, Kemmler, Roman, additional, Ritter, Sebastian, additional, Raugust, Marc, additional, Wende, Torsten, additional, Behrendt, Marcel, additional, and Regehly, Martin, additional

Published
2019
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15. Structural Basis of Vesicle Formation at the Inner Nuclear Membrane

Author

Hagen, Christoph, Dent, Kyle C., Zeev-Ben-Mordehai, Tzviya, Grange, Michael, Bosse, Jens B., Whittle, Cathy, Klupp, Barbara G., Siebert, C. Alistair, Vasishtan, Daven, Baeuerlein, Felix J. B., Cheleski, Juliana, Werner, Stephan, Guttmann, Peter, Rehbein, Stefan, Henzler, Katja, Demmerle, Justin, Adler, Barbara, Koszinowski, Ulrich, Schermelleh, Lothar, Schneider, Gerd, Enquist, Lynn W., Plitzko, Juergen M., Mettenleiter, Thomas C., and Gruenewald, Kay

Subjects
Electron Microscope Tomography, Nuclear Envelope, Biochemistry, Genetics and Molecular Biology(all), Cryoelectron Microscopy, Active Transport, Cell Nucleus, Nuclear Proteins, Herpesvirus 1, Human, Herpesvirus 1, Suid, Article, Viral Proteins, Capsid, Pyrimidine Dimers, Chlorocebus aethiops, Scattering, Small Angle, Animals, Transport Vesicles, Vero Cells
Abstract

Summary Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane. To understand the structural underpinning for this trafficking, we investigated nuclear egress of progeny herpesvirus capsids where capsid envelopment is mediated by two viral proteins, forming the nuclear egress complex (NEC). Using a multi-modal imaging approach, we visualized the NEC in situ forming coated vesicles of defined size. Cellular electron cryo-tomography revealed a protein layer showing two distinct hexagonal lattices at its membrane-proximal and membrane-distant faces, respectively. NEC coat architecture was determined by combining this information with integrative modeling using small-angle X-ray scattering data. The molecular arrangement of the NEC establishes the basic mechanism for budding and scission of tailored vesicles at the INM., Graphical Abstract, Highlights • Multimodal imaging reveals mechanism of vesicle formation at inner nuclear membrane • Nucleo-cytoplasmic cargo vesicle coat in situ comprises two distinct lattices • Lattices are formed by hexameric building blocks made of the nuclear egress complex • Induction of membrane curvature based solely on heterodimeric interactions, A multi-modal live-cell and cryo-imaging approach reveals how vesicles assemble at the inner nuclear membrane for transport to the cytoplasm during herpesvirus maturation. This also suggests a functional model for counterparts in uninfected cells that mediate nuclear egress of large cargo like ribonucleoprotein particles.

Published
2015

16. Direct images of the virtual source in a supersonic expansion

Author

Reisinger, Thomas, Bracco, Gianagelo, Rehbein, Stefan, Schmahl, Gunter, Ernst, Wolfgang E., and Holst, Bodil

Subjects
Helium -- Properties, Time-of-flight mass spectrometry -- Analysis, Molecular beams -- Usage, Chemicals, plastics and rubber industries
Abstract

The direct images of the virtual source in a supersonic expansion of helium are described by using a Fresnel zone plate with free-standing zones. The results are very important for understanding the supersonic expansion process.

Published
2007

19. Multimodal nanoparticles as alignment and correlation markers in fluorescence/soft X-ray cryo-microscopy/tomography of nucleoplasmic reticulum and apoptosis in mammalian cells

Author

Hagen, Christoph, primary, Werner, Stephan, additional, Carregal-Romero, Susana, additional, N. Malhas, Ashraf, additional, G. Klupp, Barbara, additional, Guttmann, Peter, additional, Rehbein, Stefan, additional, Henzler, Katja, additional, C. Mettenleiter, Thomas, additional, J. Vaux, David, additional, J. Parak, Wolfgang, additional, Schneider, Gerd, additional, and Grünewald, Kay, additional

Published
2014
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21. Ion beam lithography for Fresnel zone plates in X-ray microscopy

Author

Keskinbora, Kahraman, primary, Grévent, Corinne, additional, Bechtel, Michael, additional, Weigand, Markus, additional, Goering, Eberhard, additional, Nadzeyka, Achim, additional, Peto, Lloyd, additional, Rehbein, Stefan, additional, Schneider, Gerd, additional, Follath, Rolf, additional, Vila-Comamala, Joan, additional, Yan, Hanfei, additional, and Schütz, Gisela, additional

Published
2013
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25. Cryo X-ray nano-tomography of vaccinia virus infected cells

Author

Chichón, Francisco Javier, primary, Rodríguez, Maria Josefa, additional, Pereiro, Eva, additional, Chiappi, Michele, additional, Perdiguero, Beatriz, additional, Guttmann, Peter, additional, Werner, Stephan, additional, Rehbein, Stefan, additional, Schneider, Gerd, additional, Esteban, Mariano, additional, and Carrascosa, José L., additional

Published
2012
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30. Hard X Ray Holographic Diffraction Imaging

Author

Stadler, Lorenz-M., primary, Gutt, Christian, additional, Autenrieth, Tina, additional, Leupold, Olaf, additional, Rehbein, Stefan, additional, Chushkin, Yuriy, additional, and Grübel, Gerhard, additional

Published
2008
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32. Nanoscale spectroscopy with polarized X-rays by NEXAFS-TXM.

Author

Guttmann, Peter, Bittencourt, Carla, Rehbein, Stefan, Umek, Polona, Ke, Xiaoxing, Van Tendeloo, Gustaaf, Ewels, Chris P., and Schneider, Gerd

Subjects
NANOSTRUCTURES, PHOTONICS, X-rays, SPECTRUM analysis, PHOTONS
Abstract

Near-edge X-ray absorption spectroscopy (NEXAFS) is an essential analytical tool in material science. Combining NEXAFS with scanning transmission X-ray microscopy (STXM) adds spatial resolution and the possibility to study individual nanostructures. Here, we describe a full-field transmission X-ray microscope (TXM) that generates high-resolution, large-area NEXAFS data with a collection rate two orders of magnitude faster than is possible with STXM. The TXM optical design combines a spectral resolution of E/?E = 1 × 104 with a spatial resolution of 25 nm in a field of view of 15-20 µm and a data acquisition time of ?1 s. As an example, we present image stacks and polarization-dependent NEXAFS spectra from individual anisotropic sodium and protonated titanate nanoribbons. Our NEXAFS-TXM technique has the advantage that one image stack visualizes a large number of nanostructures and therefore already contains statistical information. This new high-resolution NEXAFS-TXM technique opens the way to advanced nanoscale science studies. [ABSTRACT FROM AUTHOR]

Published
2012
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34. Structural Basis of Vesicle Formation at the Inner Nuclear Membrane.

Author

Hagen C, Dent KC, Zeev-Ben-Mordehai T, Grange M, Bosse JB, Whittle C, Klupp BG, Siebert CA, Vasishtan D, Bäuerlein FJ, Cheleski J, Werner S, Guttmann P, Rehbein S, Henzler K, Demmerle J, Adler B, Koszinowski U, Schermelleh L, Schneider G, Enquist LW, Plitzko JM, Mettenleiter TC, and Grünewald K

Subjects
Animals, Capsid ultrastructure, Chlorocebus aethiops, Cryoelectron Microscopy, Electron Microscope Tomography, Herpesvirus 1, Human metabolism, Herpesvirus 1, Suid metabolism, Nuclear Envelope chemistry, Nuclear Proteins chemistry, Nuclear Proteins metabolism, Pyrimidine Dimers, Scattering, Small Angle, Transport Vesicles metabolism, Vero Cells, Viral Proteins chemistry, Viral Proteins metabolism, Active Transport, Cell Nucleus, Capsid metabolism, Nuclear Envelope metabolism, Nuclear Envelope ultrastructure, Transport Vesicles ultrastructure
Abstract

Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane. To understand the structural underpinning for this trafficking, we investigated nuclear egress of progeny herpesvirus capsids where capsid envelopment is mediated by two viral proteins, forming the nuclear egress complex (NEC). Using a multi-modal imaging approach, we visualized the NEC in situ forming coated vesicles of defined size. Cellular electron cryo-tomography revealed a protein layer showing two distinct hexagonal lattices at its membrane-proximal and membrane-distant faces, respectively. NEC coat architecture was determined by combining this information with integrative modeling using small-angle X-ray scattering data. The molecular arrangement of the NEC establishes the basic mechanism for budding and scission of tailored vesicles at the INM., (Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.)

Published
2015
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