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Showing 1–16 of 16 results
Advanced filters: Author: Valerio Mariani Clear advanced filters

  • Time-resolved crystallography (TRX) is used for monitoring only small conformational changes of biomacromolecules within the same lattice. Here, the authors report the interplay between synchronous molecular rearrangements and lattice phase transitions in RNA crystals, providing the basis for the investigation of large conformational changes using TRX.

    • Saminathan Ramakrishnan
    • Jason R. Stagno
    • Yun-Xing Wang
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10

  • EGFRvIII-targeted CAR T cells have been proposed as a therapeutic option for patients with glioblastoma (GBM), however, clinical responses remain suboptimal. Here the authors engineer anti-EGFRvIII CAR T cells to secrete an optimized SIRPγ-derived CD47 blocker, showing that combining CAR T cell effector functions with enhanced macrophage-mediated tumor cell phagocytosis improves anti-tumor efficacy in preclinical models.

    • Tomás A. Martins
    • Deniz Kaymak
    • Gregor Hutter
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-25

  • Due to the pulsed nature of X-ray free electron laser (XFEL) instruments the majority of protein crystals, which are injected using continuous jet injection techniques are wasted. Here, the authors present a microfluidic device to deliver aqueous protein crystal laden droplets segmented with an immiscible oil and demonstrate that with this device an approx. 60% reduction in sample waste was achieved for data collection of 3-deoxy-D-manno-octulosonate 8-phosphate synthase crystals at the EuXFEL.

    • Austin Echelmeier
    • Jorvani Cruz Villarreal
    • Alexandra Ros
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • The European X-ray free-electron laser (EuXFEL) in Hamburg is the first XFEL with a megahertz repetition rate. Here the authors present the 2.9 Å structure of the large membrane protein complex Photosystem I from T. elongatus that was determined at the EuXFEL.

    • Chris Gisriel
    • Jesse Coe
    • Nadia A. Zatsepin
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • Here, the reaction of the suicide inhibitor sulbactam with the M. tuberculosis β-lactamase (BlaC) is investigated with time-resolved crystallography. Singular Value Decomposition is implemented to extract kinetic information despite changes in unit cell parameters during the time-course of the reaction.

    • Tek Narsingh Malla
    • Kara Zielinski
    • Marius Schmidt
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • The new European X-Ray Free-Electron Laser (EuXFEL) is the first XFEL that generates X-ray pulses with a megahertz inter-pulse spacing. Here the authors demonstrate that high-quality and damage-free protein structures can be obtained with the currently available 1.1 MHz repetition rate pulses using lysozyme as a test case and furthermore present a β-lactamase structure.

    • Max O. Wiedorn
    • Dominik Oberthür
    • Anton Barty
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11

  • Crystal lattice disorder, which gives rise to a continuous diffraction pattern, is exploited to determine the structure of the integral membrane protein complex photosystem II to a higher resolution than could be achieved using Bragg diffraction alone.

    • Kartik Ayyer
    • Oleksandr M. Yefanov
    • Henry N. Chapman
    Research
    Nature
    Volume: 530, P: 202-206

  • Although the photocycle of the photosensory core module of the Stigmatella aurantiaca bacteriophytochrome 2 (SaBphP2) has been extensively studied, its early dynamics have not been fully resolved. Here, the authors use time-resolved serial femtosecond crystallography to probe the associated picosecond events and report on the relative population of Z and E isomers after light activation.

    • Tek Narsingh Malla
    • Luis Aldama
    • Marius Schmidt
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-10

  • Ayan et al. report two structures of the protein streptavidin - one at ambient temperature determined using serial femtosecond crystallography and a second one determined at cryogenic temperature. These results provide insights into the structural dynamics of apo streptavidin and reveal a cooperative allostery between monomers for binding to biotin, and the findings are supported by GNM analysis.

    • Esra Ayan
    • Busra Yuksel
    • Hasan DeMirci
    ResearchOpen Access
    Communications Biology
    Volume: 5, P: 1-13