Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–11 of 11 results
Advanced filters: Author: Helen M Ginn Clear advanced filters

  • Serial femtosecond crystallography and the use of X-ray free-electron lasers (XFEL) promise to revolutionize structural biology. Here, the authors describe refinements that reduce the redundancy required to obtain quality XFEL data and report a 1.75-Å structure—not obtainable by synchrotron radiation—using less than 6,000 crystals.

    • Helen M. Ginn
    • Marc Messerschmidt
    • David I. Stuart
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-8

  • Although the conformations of highly populated protein metastable states have been studied in detail, capturing the transitions between those states has remained challenging. Here, the authors present an algorithm that generates trajectories in torsion angle space by minimising the kinetic energy required for a transition between experimentally determined end states, demonstrating its application to three membrane transporter superfamilies.

    • Briony A. Yorke
    • Helen M. Ginn
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-10

  • A new sample-delivery method for serial X-ray crystallography exploits the full repetition rate of the X-ray free-electron laser at the LCLS facility, thus enabling efficient, high-speed data collection to solve the three-dimensional structures of viruses.

    • Philip Roedig
    • Helen M Ginn
    • Alke Meents
    Research
    Nature Methods
    Volume: 14, P: 805-810

  • 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

  • Understanding the stability of the eye lens protein human gamma-D crystallin (HGD) is essential to developing tools to prevent the formation of cataracts, however, structural investigations of the response of HGD to ultraviolet radiation are lacking. Here, the authors use continuous illumination serial crystallography to directly probe the mechanism of R36S HGD in response to ultraviolet radiation damage.

    • Jake A. Hill
    • Yvonne Nyathi
    • Briony A. Yorke
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-8

  • 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

  • Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen protein-protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.

    • Abhay Kotecha
    • Julian Seago
    • David I Stuart
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 788-794

  • The structures of amyloid fibres are currently primarily studied through solid state NMR and cryo-EM. Here the authors present a free-standing graphene support device that allows diffraction imaging of non-crystalline amyloid fibrils with single X-ray pulses from an X-ray free-electron laser.

    • Carolin Seuring
    • Kartik Ayyer
    • Henry N. Chapman
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10