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

DOI: 10.1038/ncomms7435 DOI Help
PMID: 25751308 PMID Help

Authors: Helen M Ginn (University of Oxford) , Marc Messerschmidt (SLAC) , Xiaoyun Ji (University of Oxford) , Hanwen Zhang (University of Oxford) , Danny Axford (Diamond Light Source) , Richard J Gildea (Diamond Light Source) , Graeme Winter (Diamond Light Source) , Aaron S. Brewster (Lawrence Berkeley National Laboratory) , Johan Hattne (Lawrence Berkeley National Laboratory) , Armin Wagner (Diamond Light Source) , Jonathan M Grimes (Division of Structural Biology, University of Oxford) , Gwyndaf Evans (Diamond Light Source) , Nicholas K. Sauter (Lawrence Berkeley National Laboratory) , Geoff Sutton (University of Oxford) , David I Stuart (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 6

State: Published (Approved)
Published: March 2015

Open Access Open Access

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.

Journal Keywords: Biological Sciences; Biophysics; Virology

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: SLAC

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