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

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, Nicholas K. Sauter, Geoff Sutton and David I. Stuart ()
Additional contact information
Helen M. Ginn: The Wellcome Trust Centre for Human Genetics, University of Oxford
Marc Messerschmidt: SLAC National Accelerator Laboratory
Xiaoyun Ji: The Wellcome Trust Centre for Human Genetics, University of Oxford
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
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

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms7435

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