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Structure of CPV17 polyhedrin determined by the improved analysis of serial femtosecond crystallographic data

Author

Listed:
  • Helen M. Ginn

    (The Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Marc Messerschmidt

    (SLAC National Accelerator Laboratory
    Present address: National Science Foundation BioXFEL Science and Technology Center, 700 Ellicott Street, Buffalo, New York 14203, USA)

  • Xiaoyun Ji

    (The Wellcome Trust Centre for Human Genetics, University of Oxford
    Molecular Biophysics and Biochemistry, Yale School of Medicine, 333 Cedar Street, New Haven, Connecticut 06510, USA)

  • Hanwen Zhang

    (The Wellcome Trust Centre for Human Genetics, University of Oxford)

  • Danny Axford

    (Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

  • Richard J. Gildea

    (Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

  • Graeme Winter

    (Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

  • Aaron S. Brewster

    (Lawrence Berkeley National Laboratory)

  • Johan Hattne

    (Lawrence Berkeley National Laboratory)

  • Armin Wagner

    (Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

  • Jonathan M. Grimes

    (The Wellcome Trust Centre for Human Genetics, University of Oxford
    Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

  • Gwyndaf Evans

    (Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

  • Nicholas K. Sauter

    (Lawrence Berkeley National Laboratory)

  • Geoff Sutton

    (The Wellcome Trust Centre for Human Genetics, University of Oxford)

  • David I. Stuart

    (The Wellcome Trust Centre for Human Genetics, University of Oxford
    Diamond House, Diamond Light Source, Harwell Science & Innovation Campus)

Abstract

The X-ray free-electron laser (XFEL) allows the analysis of small weakly diffracting protein crystals, but has required very many crystals to obtain good data. Here we use an XFEL to determine the room temperature atomic structure for the smallest cytoplasmic polyhedrosis virus polyhedra yet characterized, which we failed to solve at a synchrotron. These protein microcrystals, roughly a micron across, accrue within infected cells. We use a new physical model for XFEL diffraction, which better estimates the experimental signal, delivering a high-resolution XFEL structure (1.75 Å), using fewer crystals than previously required for this resolution. The crystal lattice and protein core are conserved compared with a polyhedrin with less than 10% sequence identity. We explain how the conserved biological phenotype, the crystal lattice, is maintained in the face of extreme environmental challenge and massive evolutionary divergence. Our improved methods should open up more challenging biological samples to XFEL analysis.

Suggested Citation

  • Helen M. Ginn & Marc Messerschmidt & Xiaoyun Ji & Hanwen Zhang & Danny Axford & Richard J. Gildea & Graeme Winter & Aaron S. Brewster & Johan Hattne & Armin Wagner & Jonathan M. Grimes & Gwyndaf Evans, 2015. "Structure of CPV17 polyhedrin determined by the improved analysis of serial femtosecond crystallographic data," Nature Communications, Nature, vol. 6(1), pages 1-8, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7435
    DOI: 10.1038/ncomms7435
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    Cited by:

    1. Jeremy R. Keown & Adam D. Crawshaw & Jose Trincao & Loïc Carrique & Richard J. Gildea & Sam Horrell & Anna J. Warren & Danny Axford & Robin Owen & Gwyndaf Evans & Annie Bézier & Peter Metcalf & Jonath, 2023. "Atomic structure of a nudivirus occlusion body protein determined from a 70-year-old crystal sample," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Robert Schönherr & Juliane Boger & J. Mia Lahey-Rudolph & Mareike Harms & Jacqueline Kaiser & Sophie Nachtschatt & Marla Wobbe & Rainer Duden & Peter König & Gleb Bourenkov & Thomas R. Schneider & Lar, 2024. "A streamlined approach to structure elucidation using in cellulo crystallized recombinant proteins, InCellCryst," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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