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Showing 1–11 of 11 results
Advanced filters: Author: Ludovic Renault Clear advanced filters

  • Retroviral integrases catalyze the insertion of viral DNA into the host cell DNA and can use nucleosomes as substrates for integration. Here the authors present the 3.9 Å cryo-EM structure of prototype foamy virus integrase after strand transfer into nucleosomal DNA, which together with single-molecule FRET measurements provides evidence for a DNA looping and sliding mechanism of integrases.

    • Marcus D. Wilson
    • Ludovic Renault
    • Alessandro Costa
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • The Cdc45-MCM-GINS (CMG) helicase unwinds DNA during replication, a process that requires the ATPase-dependent activity of the MCM complex. Using cryo-EM reconstructions of the CMG complex in different conformations, the authors propose a model where the N-terminal and AAA+ domains of MCM work in concert to translocate along DNA.

    • Ferdos Abid Ali
    • Ludovic Renault
    • Alessandro Costa
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-11

  • Faster cryo specimen preparation can advance cryo electron microscopy (cryoEM). Here, the authors present a vitrification device with automated sample handling for cryoEM of proteins, suspensions and cells, enabling blot-free sample thinning, dew-point control and characterization of cryo grids prior to data acquisition.

    • Roman I. Koning
    • Hildo Vader
    • Michael Schwertner
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • SARS-CoV-2 S protein prematurely refolds to the post-fusion conformation, compromising immunogenic properties and prefusion trimer yield. Here, Juraszek et al. present a stable SARS-CoV-2 S-closed protein variant with increased expression and correct folding, predominantly in closed prefusion conformation.

    • Jarek Juraszek
    • Lucy Rutten
    • Johannes P. M. Langedijk
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-8

  • The loading and activation of the Mcm2-7 replicative helicase couples cell cycle progression to DNA replication. Here the authors use X-ray crystallography and single-particle electron microscopy to demonstrate how Ctd1 functions to promote MCM loading onto DNA.

    • Jordi Frigola
    • Jun He
    • John F. X. Diffley
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10

  • Retroviruses such as HIV rely on the intasome, a tetramer of integrase protein bound to the viral DNA ends interacting with host chromatin, for integration into the host genome; the structure of the intasome as it interacts with a nucleosome is now solved, giving insight into the integration process.

    • Daniel P. Maskell
    • Ludovic Renault
    • Peter Cherepanov
    Research
    Nature
    Volume: 523, P: 366-369

  • This study shows how the yeast Ctf4 protein couples the DNA helicase, Cdc45–MCM–GINS, to DNA polymerase α — the GINS subunit of the helicase and the polymerase use a similar interaction to bind Ctf4, suggesting that, as Ctf4 is a trimer, two polymerases could be simultaneously coupled to a single helicase during lagging-strand synthesis.

    • Aline C. Simon
    • Jin C. Zhou
    • Luca Pellegrini
    Research
    Nature
    Volume: 510, P: 293-297

  • Depelteau et al. present a new method to inactivate cryo-EM samples from pathogenic organisms before imaging using ultraviolet-C radiation in cryogenic conditions. This method allows for the inexpensive preparation of cryo-EM samples with no discernable structural impact of the treatment.

    • Jamie S. Depelteau
    • Ludovic Renault
    • Ariane Briegel
    ResearchOpen Access
    Communications Biology
    Volume: 5, P: 1-8

  • A collection of 131 multi-panel pediatric tumor PDX models are generated and characterized in a comprehensive effort to provide support for basic and translational research and treatment development in advanced pediatric malignancies.

    • Maria Eugénia Marques Da Costa
    • Sakina Zaidi
    • Birgit Geoerger
    ResearchOpen Access
    Communications Biology
    Volume: 6, P: 1-15