Vogt, Majbritt

[["dc.bibliographiccitation.firstpage","607"],["dc.bibliographiccitation.journal","Journal de Physique. IV, Proceedings"],["dc.bibliographiccitation.lastpage","613"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Denbeaux, G."],["dc.contributor.author","Anderson, E."],["dc.contributor.author","Pearson, A."],["dc.contributor.author","Bates, W."],["dc.contributor.author","Vogt, S."],["dc.contributor.author","Knochel, C."],["dc.contributor.author","Meyer, M. A."],["dc.contributor.author","Zschech, E."],["dc.date.accessioned","2018-11-07T10:40:32Z"],["dc.date.available","2018-11-07T10:40:32Z"],["dc.date.issued","2003"],["dc.description.abstract","With the new tomography setup developed for the x-ray microscope XM-1 installed at the Advanced Light Source, tomography of immunolabelled frozen-hydrated cells to detect protein distributions inside of cells was performed. The distribution of the nuclear protein, male specific lethal 1 (MSL-1) in the Drosophila melanogaster cell was studied. Another application field for high resolution tomography which is of fundamental interest in materials science is electromigration in advanced copper interconnects. In this work, quantitative time-resolved x-ray microscopy mass transport studies of the early stages of electromigration in an inlaid Cu line/via structure were performed with 40 nm spatial resolution at 1.8 keV photon energy. Correlation of the real time x-ray microscopy images with post mortem high voltage electron micrographs of the sample shows that the void nucleation occurs at the site of grain boundaries in Cu and that the voids migrate along these grain boundaries during electromigration. To provide 3D information about the exact location (bulk or interface) of void nucleation and migration during an EM experiment, as well as to measure quantitatively the mass transport in the volume, future experiments must be based on time-resolved x-ray tomography."],["dc.identifier.doi","10.1051/jp4:20030155"],["dc.identifier.isi","000183273900142"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46323"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.conference","7th International Conference on X-Ray Microscopy"],["dc.relation.eventlocation","GRENOBLE, FRANCE"],["dc.relation.issn","1155-4339"],["dc.title","High resolution X-ray tomography with applications in biology and materials science"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1308"],["dc.bibliographiccitation.journal","NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT"],["dc.bibliographiccitation.lastpage","1311"],["dc.bibliographiccitation.volume","467"],["dc.contributor.author","Weiss, D."],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Vogt, S."],["dc.contributor.author","Guttmann, Peter"],["dc.contributor.author","Niemann, B."],["dc.contributor.author","Rudolph, D."],["dc.contributor.author","Schmahl, G."],["dc.date.accessioned","2018-11-07T08:52:03Z"],["dc.date.available","2018-11-07T08:52:03Z"],["dc.date.issued","2001"],["dc.description.abstract","Using the photoelectric absorption contrast between water and protein at 2.4 nm wavelength, cryo X-ray microscopy has visualized protein structures down to 30 mn size in unstained, unsectioned biological specimens. Due to the large depth of focus of the Fresnel zone plate objectives, computed tomography based on a tilt series of X-ray microscopic images can be used to reconstruct the three-dimensional specimen structure. This method has been applied to the green alga Chlamydomonas reinhardtii, and to cell nuclei of male Drosophila melanogaster fruit fly cells. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0168-9002(01)00648-9"],["dc.identifier.isi","000171012800114"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22075"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.conference","7th International Conference on Synchrotron Radiation Instrumentation (SRI 2000)"],["dc.relation.eventlocation","TECH UNIV BERLIN, BERLIN, GERMANY"],["dc.relation.issn","0168-9002"],["dc.title","Tomographic imaging of biological specimens with the cryo transmission X-ray microscope"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1312"],["dc.bibliographiccitation.journal","NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT"],["dc.bibliographiccitation.lastpage","1314"],["dc.bibliographiccitation.volume","467"],["dc.contributor.author","Vogt, S."],["dc.contributor.author","Jager, Martin"],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Schulze, E."],["dc.contributor.author","Saumweber, H."],["dc.contributor.author","Rudolph, D."],["dc.contributor.author","Schmahl, G."],["dc.date.accessioned","2018-11-07T08:52:05Z"],["dc.date.available","2018-11-07T08:52:05Z"],["dc.date.issued","2001"],["dc.description.abstract","Specific nuclear proteins in immunogold labeled Drosophila melanogaster cells were visualized by applying soft X-ray microscopy. In addition, first experiments were performed to localize two different labeled nuclear proteins in the same X-ray micrograph by using immunofluorescence microscopy for distinguishing the proteins. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0168-9002(01)00650-7"],["dc.identifier.isi","000171012800115"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22085"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.conference","7th International Conference on Synchrotron Radiation Instrumentation (SRI 2000)"],["dc.relation.eventlocation","TECH UNIV BERLIN, BERLIN, GERMANY"],["dc.relation.issn","0168-9002"],["dc.title","Visualizing specific nuclear proteins in eukaryotic cells using soft X-ray microscopy"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","177"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Surface Review and Letters"],["dc.bibliographiccitation.lastpage","183"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Anderson, E."],["dc.contributor.author","Vogt, S."],["dc.contributor.author","Knochel, C."],["dc.contributor.author","Weiss, D."],["dc.contributor.author","Legros, M."],["dc.contributor.author","Larabell, C."],["dc.date.accessioned","2018-11-07T10:32:27Z"],["dc.date.available","2018-11-07T10:32:27Z"],["dc.date.issued","2002"],["dc.description.abstract","Soft X-ray microscopy has resolved 30 nm structures in biological cells. To protect the cells from radiation damage caused by X-rays, imaging of the samples has to be performed at cryogenic temperatures, which makes it possible to take multiple images of a single cell. Due to the small numerical aperture of zone plates, X-ray objectives have a depth of focus on the order of several microns. By treating the X-ray microscopic images as projections of the sample absorption, computed tomography (CT) can be performed. Since cryogenic biological samples are resistant to radiation damage, it is possible to reconstruct frozen-hydrated cells imaged with a full-field X-ray microscope. This approach is used to obtain three-dimensional information about the location of specific proteins in cells. To localize proteins in cells, immunolabeling with strongly X-ray absorbing nanoparticles was performed. With the new tomography setup developed for the X-ray microscope XM-1 installed at the ALS, we have performed tomography of immunolabeled frozen-hydrated cells to detect protein distributions inside of cells. As a first example, the distribution of the nuclear protein male-specific lethal 1 (MSL-1) in the Drosophila melanogaster cell was studied."],["dc.identifier.doi","10.1142/S0218625X02001914"],["dc.identifier.isi","000177754500029"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44347"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","World Scientific Publ Co Pte Ltd"],["dc.publisher.place","Singapore"],["dc.relation.conference","13th International Conference on Vacuum Ultraviolet Radiation Physics (VUV-13)"],["dc.relation.eventlocation","TRIESTE, ITALY"],["dc.relation.issn","0218-625X"],["dc.title","Computed tomography of cryogenic cells"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]