Frank Schlünzen

Deutsches Elektronen-Synchrotron DESY

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J. Harms

University of California, Berkeley

Ada Yonath

Weizmann Institute of Science

Heike Bartels

Weizmann Institute of Science

F. Franceschi

Global Antibiotic Research & Development Partnership

Harly A. S. Hansen

Max Planck Institute for Molecular Genetics

Ilana Agmon

Technion – Israel Institute of Technology

Anat Bashan

Weizmann Institute of Science

William S. Bennett

Yale University

S. Weinstein

Max Planck Unit for Structural Molecular Biology

Inna Levin

Ferring Pharmaceuticals (Switzerland)

Cooperative Institutions

Universität Hamburg

Deutsches Elektronen-Synchrotron DESY

Center for Free-Electron Laser Science

Max Planck Institute for Molecular Genetics

Weizmann Institute of Science

Max Planck Institute for the Structure and Dynamics of Matter

Max Planck Unit for Structural Molecular Biology

Max Planck Society

Hamburg Centre for Ultrafast Imaging

European X-Ray Free-Electron Laser

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SnapShot: Antibiotic Inhibition of Protein Synthesis I

Cell (2009)

Daniel Sohmen Joerg Harms Frank Schlünzen Daniel N. Wilson

Snapshot (computer storage)

10.1016/j.cell.2009.08.001

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Citations (34)

Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria

Nature (2001)

Frank Schlünzen Raz Zarivach J. Harms Anat Bashan Ante Tocilj

Peptidyl transferase

50S

23S ribosomal RNA

10.1038/35101544

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Citations (1,016)

Artificial intelligence for synchrotron-radiation tomography

Julian Moosmann Bashir Kazimi Philipp Heuser Frank Schlünzen Ivo M. Baltruschat

The Helmholtz-Zentrum Hereon is operating imaging beamlines for X-ray tomography (P05 IBL, P07 HEMS) for academic and industrial users at the synchrotron radiation source PETRA III at DESY in Hamburg, Germany. The high X-ray flux density and coherence of synchrotron radiation enables high-resolution in situ/operando/vivo tomography experiments and provides phase contrast, respectively. Large amounts of 3D/4D data are collected that are difficult to process and analyze. Here, we report on the application of machine learning for image segmentation including a guided interactive framework, multimodal data analysis (virtual histology), image enhancement (denoising), and self-supervised learning for phase retrieval.

DESY

10.1117/12.2675628

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The Knizhnik-Polyakov-Zamolodchikov equation in induced quantum (super)gravity

Classical and Quantum Gravity (1990)

Frank Schlünzen

The Knizhnik-Polyakov-Zamolodchikov equation of induced quantum gravity is derived in a rather simple way. The construction is generalised to N=1, 2 and 4 supergravity.

Spin foam

10.1088/0264-9381/7/8/018

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Citations (2)

Data collected and evaluated from crystals of ribosomal particles

Acta Crystallographica Section A Foundations of Crystallography (1993)

Ilana Agmon Heike Bartels William S. Bennett Z. Berkovitch‐Yellin K. von Böhlen

10.1107/s0108767378096713

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Crystallographic Studies on the Ribosome, a Large Macromolecular Assembly Exhibiting Severe Nonisomorphism, Extreme Beam Sensitivity and No Internal Symmetry

Acta Crystallographica Section A Foundations of Crystallography (1998)

Ada Yonath J. Harms Harly A. S. Hansen Anat Bashan Frank Schlünzen

Crystals, diffracting best to around 3 Å, have been grown from intact large and small ribosomal subunits. The bright synchrotron radiation necessary for the collection of the higher-resolution X-ray diffraction data introduces significant decay even at cryo temperatures. Nevertheless, owing to the reasonable isomorphism of the recently improved crystals of the small ribosomal subunits, reliable phases have been extracted at medium resolution (5–6 Å) and an interpretable five-derivative MIR map has been constructed. For the crystals of the large subunits, however, the situation is more complicated because at higher resolution (2.7–7 Å) they suffer from substantial radiation sensitivity, a low level of isomorphism, instability of the longest unit-cell axis and nonisotropic mosaicity. The 8 Å MIR map, constructed to gain insight into this unusual system, may provide feasible reasoning for the odd combination of the properties of these crystals as well as hints for future improvement. Parallel efforts, in which electron-microscopy-reconstructed images are being exploited for molecular-replacement studies, are also discussed.

Mosaicity

Isomorphism (crystallography)

10.1107/s010876739800991x

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Citations (72)

Structural Basis for the Function of the Ribosomal L7/12 Stalk in Factor Binding and GTPase Activation

Cell (2005)

Mihaela Diaconu Ute Kothe Frank Schlünzen N. Fischer J. Harms

Stalk

Basis (linear algebra)

10.1016/j.cell.2005.04.015

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Citations (421)

Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin

Molecular Microbiology (2004)

Frank Schlünzen Erez Pyetan Paola Fucini Ada Yonath J. Harms

Tiamulin, a prominent member of the pleuromutilin class of antibiotics, is a potent inhibitor of protein synthesis in bacteria. Up to now the effect of pleuromutilins on the ribosome has not been determined on a molecular level. The 3.5 A structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin provides for the first time a detailed picture of its interactions with the 23S rRNA, thus explaining the molecular mechanism of the antimicrobial activity of the pleuromutilin class of antibiotics. Our results show that tiamulin is located within the peptidyl transferase center (PTC) of the 50S ribosomal subunit with its tricyclic mutilin core positioned in a tight pocket at the A-tRNA binding site. Also, the extension, which protrudes from its mutilin core, partially overlaps with the P-tRNA binding site. Thereby, tiamulin directly inhibits peptide bond formation. Comparison of the tiamulin binding site with other PTC targeting drugs, like chloramphenicol, clindamycin and streptogramins, may facilitate the design of modified or hybridized drugs that extend the applicability of this class of antibiotics.

Tiamulin

Peptidyl transferase

23S ribosomal RNA

50S

Ribosomal protein

10.1111/j.1365-2958.2004.04346.x

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Citations (232)

Initial phasing in ribosomal crystallography

Acta Crystallographica Section A Foundations of Crystallography (1996)

Z. Berkovitch‐Yellin Ilana Agmon Konstantinos Anagnostopoulos Heike Bartels Anat Bashan

Phaser