Zobrazeno 1 - 10
of 134
pro vyhledávání: '"F. Zemlin"'
Autor:
F. Zemlin, E. Beckmann, Rudi Lurz, Elena V. Orlova, Prakash Dube, Thomas A. Trautner, Paulo Tavares, Marin van Heel
Publikováno v:
Nature Structural Biology. 6:842-846
We have determined the three-dimensional structure of bacteriophage SPP1 portal protein (gp6) using electron microscopy at liquid-helium temperatures and angular reconstitution. The 13-fold symmetric gp6 oligomer is a turbine-shaped structure with th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c947b79af2783da2df38606ada07e75a
https://doi.org/10.1038/12303
https://doi.org/10.1038/12303
Autor:
F. Zemlin
Publikováno v:
Crystal Research and Technology. 33:1097-1111
This tutorial paper is the mannscript of a lecture given in the Harnack-Haus in Berlin during the antumn school 1998 on Metal Clusters. The aim of this lecture was to give some hints for quantitative electron microscopy. The interpretation of electro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4910f9f0026b28adaf255a80af636c7
https://doi.org/10.1002/(sici)1521-4079(199810)33:7/8<1097::aid-crat1097>3.0.co
https://doi.org/10.1002/(sici)1521-4079(199810)33:7/8<1097::aid-crat1097>3.0.co
Autor:
Prakash Dube, Richard Brimacombe, Holger Stark, Florian Mueller, Marin van Heel, Gerald Bacher, F. Zemlin
Publikováno v:
Journal of Molecular Biology. 279:403-421
Samples of 80 S ribosomes from rabbit reticulocytes were subjected to electron cryomicroscopy combined with angular reconstitution. A three-dimensional reconstruction at 21 A resolution was obtained, which was compared with the corresponding (previou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73ee02bbd2c624180c2c6c7bc95e10af
https://doi.org/10.1006/jmbi.1998.1804
https://doi.org/10.1006/jmbi.1998.1804
Autor:
Michael Schatz, Prakash Dube, Gudrun Lutsch, Holger Stark, Martin Wieske, F. Zemlin, Marin van Heel, Joachim Stahl
Publikováno v:
Scopus-Elsevier
Background: The ribosome is central to protein synthesis in all living organisms. Single-particle electron cryomicroscopy has recently led to the determination of three-dimensional structures of bacterial ribosomes to ∼20 a, which have since revolu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21ef9cce69eaf8381c6eefcf0b8d17c1
Publikováno v:
Proceedings of the Royal Society of London. Series A: Mathematical, Physical and Engineering Sciences. 453:1929-1946
Lattice images of dislocations, growth boundaries and surface structure, of the n-paraffin series have been obtained by high resolution electron microscopy. The crystals were grown so that the chai...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89d4c1f39d7882c8b165e507f3145c42
https://doi.org/10.1098/rspa.1997.0104
https://doi.org/10.1098/rspa.1997.0104
Autor:
Erich Beckman, F. Zemlin, Marin van Heel, Elena V. Orlova, Jürgen Markl, J. Robin Harris, Prakash Dube
Publikováno v:
Journal of Molecular Biology. 271:417-437
A three-dimensional reconstruction of keyhole limpet hemocyanin type 1 (KLH1) has been obtained using electron cryomicroscopy at liquid helium temperatures and single particle image processing. The use of a high-contrast embedding medium, 1% (w/v) gl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf32553f09df1568d5abfe6a8ce734e1
https://doi.org/10.1006/jmbi.1997.1182
https://doi.org/10.1006/jmbi.1997.1182
Publikováno v:
Ultramicroscopy. 63:227-238
Electron microscopy of biological structural research has made significant advances. These advances were the stimulus to develop an electron microscope containing most of the desirable features and methods for high resolution cryo-electron microscopy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d677543592d665b9f4f5a671810494c
https://doi.org/10.1016/0304-3991(96)00038-1
https://doi.org/10.1016/0304-3991(96)00038-1
Publikováno v:
Ultramicroscopy. 63:75-79
A series of diffraction patterns from two-dimensional protein crystals of bacteriorhodopsin (purple membrane) at different temperatures (294 K, 98 K and 4 K) were recorded as the diffraction spots faded due to radiation damage. The patterns were then
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2d606a6c354a2670599923e63537069
https://doi.org/10.1016/0304-3991(96)00045-9
https://doi.org/10.1016/0304-3991(96)00045-9
Publikováno v:
Journal of Molecular Biology. 254:404-415
A high resolution projection at 2.6 A of deoxycholate-treated purple membrane using only images has been obtained with a 200 keV FEG microscope operated at liquid helium temperature. Examination of this high quality map has allowed the following conc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30709fab892f3d294113ab4863b10713
https://doi.org/10.1006/jmbi.1995.0627
https://doi.org/10.1006/jmbi.1995.0627
Autor:
Harald Werner, Bernd Tesche, Thilo Belz, Ursula Klengler, F. Zemlin, Armin Reller, Robert Schlögl, Elmar Zeitler, Michael Wesemann
Publikováno v:
Angewandte Chemie International Edition in English. 33:1866-1869
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5344bbc17d8eaca05e3e3d8fd38f9791
https://doi.org/10.1002/anie.199418661
https://doi.org/10.1002/anie.199418661