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Showing 1–14 of 14 results
Advanced filters: Author: Wim J. H. Hagen Clear advanced filters
  • Here the authors systematically benchmark cryo-electron tomography acquisition schemes to optimize the attainable resolution for subtomogram averaging, and find that dose-symmetric acquisition with even angular sampling provides a better outcome than most currently used acquisition schemes.

    • Beata Turoňová
    • Wim J. H. Hagen
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-9
  • A 3.3-Å-resolution cryo-EM structure of yeast Maf1 bound to RNA polymerase III (Pol III) explains the molecular mechanism for Pol III inhibition.

    • Matthias K. Vorländer
    • Florence Baudin
    • Christoph W. Müller
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 229-232
  • Globins are best known for their role in respiration, but recent studies suggest they might contribute to redox signalling as well. Here, the authors present biochemical, structural and in vivoevidence that the roundworm globin Glb-12 acts as a superoxide generator necessary for germline development.

    • Sasha De Henau
    • Lesley Tilleman
    • Bart P. Braeckman
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-14
  • PB1-mediated oligomerization of p62/SQSTM1 is essential for its function as a selective autophagy receptor. Here the authors present the cryo-EM structures of human and Arabidopsis PB1 domain helical assemblies and find that a conserved double arginine finger in the PB1 domain is important for p62 polymerisation and lysosomal targeting of p62.

    • Arjen J. Jakobi
    • Stefan T. Huber
    • Carsten Sachse
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-15
  • In-cell structural studies in Saccharomyces cerevisiae reveal that the configuration of the Nup159 complex is a key determinant of the mRNA export function of the nuclear pore complex, and suggest a model in which nuclear pore complexes are degraded via the autophagy machinery.

    • Matteo Allegretti
    • Christian E. Zimmerli
    • Martin Beck
    Research
    Nature
    Volume: 586, P: 796-800
  • RNA polymerase III (Pol III), the largest eukaryote polymerase yet characterized, transcribes structured small non-coding RNAs; here cryo-electron microscopy structures of budding yeast Pol III allow building of an atomic-level model of the complete 17-subunit complex, both unbound and while elongating RNA.

    • Niklas A. Hoffmann
    • Arjen J. Jakobi
    • Christoph W. Müller
    Research
    Nature
    Volume: 528, P: 231-236
  • Cryo-EM structures of Pol III preinitiation complexes are presented, comprising Pol III and the transcription factor TFIIIB bound to a natural promoter in different functional states.

    • Matthias K. Vorländer
    • Heena Khatter
    • Christoph W. Müller
    Research
    Nature
    Volume: 553, P: 295-300
  • The S-layer structure of C. crescentus is revealed by combining the X-ray crystal structure of an S-layer protein and cryo-ET of cell stalks. The resulting model shows that the S-layer is porous and stabilized by calcium ions.

    • Tanmay A. M. Bharat
    • Danguole Kureisaite-Ciziene
    • Jan Löwe
    Research
    Nature Microbiology
    Volume: 2, P: 1-6
  • The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization.

    • Alexander von Appen
    • Jan Kosinski
    • Martin Beck
    Research
    Nature
    Volume: 526, P: 140-143
  • Py-EM and SerialEM enable automated microscope control for high-throughput data acquisition in diverse transmission electron microscopy imaging experiments.

    • Martin Schorb
    • Isabella Haberbosch
    • David N. Mastronarde
    Reviews
    Nature Methods
    Volume: 16, P: 471-477