Rudolph, Dietbert H.

[["dc.bibliographiccitation.firstpage","123"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","132"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Vogt, S."],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Steuernagel, A."],["dc.contributor.author","Lucchesi, J."],["dc.contributor.author","Schulze, E."],["dc.contributor.author","Rudolph, D."],["dc.contributor.author","Schmahl, G."],["dc.date.accessioned","2018-11-07T08:33:41Z"],["dc.date.available","2018-11-07T08:33:41Z"],["dc.date.issued","2000"],["dc.description.abstract","X-ray microscopy is applied to detect specific proteins in whole cell nuclei of Drosophila melanogaster using immunogold labeling and silver enhancement. As a model for a small subnuclear structure the Drosophila dosage compensation protein MSL-1 was chosen. It associates with a number of other proteins to form a hetero-multiprotein complex, which elevates the transcriptional activity of the single X chromosome in males. This phenomenon is known as dosage compensation and is essential for the survival of male flies. The distribution of the Drosophila dosage compensation complex was studied by X-ray microscopy, because though the complex is expected to function by remodeling the structure of chromatin, its exact mode of action is not yet known. Many similar protein complexes are associated with different aspects of chromatin-mediated gene regulation in all eucaryotic organisms and can also be studied with the approach presented in this work. The distribution of MSL-1 protein in the nuclei of fixed D, melanogaster culture cells is visualized using the Gottingen X-ray microscope at the electron storage ring BESSY I. In addition to conventional and confocal laserscan fluorescence microscopy, X-ray microscopic investigations were performed at room as well as at cryogenic temperatures. The label can clearly be identified in the X-ray micrographs and shows detailed structure in the cell nuclei. Currently, X-ray micrographs show details in the cell nuclei about five times smaller than those in visible light micrographs. (C) 2000 Academic Press."],["dc.identifier.doi","10.1006/jsbi.2000.4277"],["dc.identifier.isi","167116800005"],["dc.identifier.pmid","11162734"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17638"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1047-8477"],["dc.title","X-ray microscopic studies of the Drosophila dosage compensation complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","849"],["dc.bibliographiccitation.journal","NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT"],["dc.bibliographiccitation.lastpage","852"],["dc.bibliographiccitation.volume","467"],["dc.contributor.author","Guttmann, Peter"],["dc.contributor.author","Niemann, B."],["dc.contributor.author","Thieme, Juergen"],["dc.contributor.author","Hambach, D."],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Wiesemann, U."],["dc.contributor.author","Rudolph, D."],["dc.contributor.author","Schmahl, Günther A."],["dc.date.accessioned","2018-11-07T08:51:43Z"],["dc.date.available","2018-11-07T08:51:43Z"],["dc.date.issued","2001"],["dc.description.abstract","A new X-ray microscopic area is going to be established at the undulator U41 at BESSY II. This undulator provides an X-ray source of high brilliance in the energy range from 163 to 595 eV in the first harmonic. The microscopic area will comprise a transmission X-ray microscope, a scanning transmission X-ray microscope, and an X-ray test chamber. (C) 2001 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0168-9002(01)00490-9"],["dc.identifier.isi","000171012800004"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22006"],["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","Instrumentation advances with the new X-ray microscopes at BESSY II"],["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","185"],["dc.bibliographiccitation.issue","3-4"],["dc.bibliographiccitation.journal","Ultramicroscopy"],["dc.bibliographiccitation.lastpage","197"],["dc.bibliographiccitation.volume","84"],["dc.contributor.author","Weiss, D."],["dc.contributor.author","Schneider, G."],["dc.contributor.author","Niemann, B."],["dc.contributor.author","Guttmann, Peter"],["dc.contributor.author","Rudolph, D."],["dc.contributor.author","Schmahl, G."],["dc.date.accessioned","2018-11-07T10:39:00Z"],["dc.date.available","2018-11-07T10:39:00Z"],["dc.date.issued","2000"],["dc.description.abstract","Soft X-ray microscopy employs the photoelectric absorption contrast between water and protein in the 2.34-4.38 nm wavelength region to visualize protein structures down to 30 nm size without any staining methods. Due to the large depth of focus of the Fresnel zone plates used as X-ray objectives, computed tomography based on the X-ray microscopic images can be used to reconstruct the local linear absorption coefficient inside the three-dimensional specimen volume. High-resolution X-ray images require a high specimen radiation dose, and a series of images taken at different viewing angles is needed for computed tomography. Therefore, cryo microscopy is necessary to preserve the structural integrity of hydrated biological specimens during image acquisition. The cryo transmission X-ray microscope at the electron storage ring BESSY I (Berlin) was used to obtain a tilt series of images of the frozen-hydrated green alga Chlamydomonas reinhardtii. The living specimens were inserted into borosilicate glass capillaries and, in this first experiment. rapidly cooled by plunging into liquid nitrogen. The capillary specimen holders allow image acquisition over the full angular range of 180 degrees. The reconstruction shows for the first time details down to 60 nm size inside a frozen-hydrated biological specimen and conveys a clear impression of the internal structures. This technique is expected to be applicable to a wide range of biological specimens, such as the cell nucleus. It offers the possibility of imaging the three-dimensional structure of hydrated biological specimens close to their natural living state. (C) 2000 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0304-3991(00)00034-6"],["dc.identifier.isi","000088612300007"],["dc.identifier.pmid","10945329"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45941"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0304-3991"],["dc.title","Computed tomography of cryogenic biological specimens based on X-ray microscopic images"],["dc.type","journal_article"],["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"]]