F
F. Zemlin
Researcher at Fritz Haber Institute of the Max Planck Society
Publications - 45
Citations - 4862
F. Zemlin is an academic researcher from Fritz Haber Institute of the Max Planck Society. The author has contributed to research in topics: Microscope & Bacteriorhodopsin. The author has an hindex of 23, co-authored 45 publications receiving 4784 citations.
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Journal ArticleDOI
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy.
TL;DR: A complete atomic model for bacteriorhodopsin between amino acid residues 8 and 225 has been built and suggests that pK changes in the Schiff base must act as the means by which light energy is converted into proton pumping pressure in the channel.
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Coma-free alignment of high-resolution electron microscopes with the aid of optical diffractograms
TL;DR: In this paper, a transmission electron microscope with a single field condenser objective is used to align the microscope onto the coma-free and dispersion-free pencil axis and does not rely on current commutation.
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The 70S Escherichia coli ribosome at 23 A resolution: fitting the ribosomal RNA.
Holger Stark,Florian Mueller,Elena V. Orlova,Michael Schatz,Prakash Dube,Tarik Erdemir,F. Zemlin,Richard Brimacombe,Marin van Heel +8 more
TL;DR: The 23 A resolution map of the 70S ribosome elucidates many structural details, such as an extensive system of channels within the 50S subunit and an intersubunit gap ideally shaped to accommodate two transfer RNA molecules.
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Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 A resolution by electron cryomicroscopy and angular reconstitution.
Elena V. Orlova,Elena V. Orlova,Prakash Dube,Prakash Dube,J. Robin Harris,Erich Beckman,F. Zemlin,Jürgen Markl,Marin van Heel +8 more
TL;DR: 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, which shows much detail and reveals many new symmetry elements in this very large cylindrical molluscan hemOCyanin.
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Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
Holger Stark,Marina V. Rodnina,Hans-Joachim Wieden,F. Zemlin,Wolfgang Wintermeyer,M. van Heel +5 more
TL;DR: The 13 Å resolution three-dimensional reconstruction determined by cryo-electron microscopy of the kirromycin-stalled codon-recognition complex provides a detailed snapshot view of an important functional state of the ribosome and suggest mechanisms of decoding and GTPase activation.