4QX1 : Cry3A Toxin structure obtained by Serial Femtosecond Crystallography from in vivo grown crystals isolated from Bacillus thuringiensis and data processed with the CrystFEL software suite

  • Michael R. Sawaya (Contributor)
  • Duilio Cascio (Contributor)
  • Mari Gingery (Contributor)
  • Jose Rodriguez (Contributor)
  • Lukasz Goldschmidt (Contributor)
  • Jacques Philippe Colletier (Contributor)
  • Marc Messerschmidt (Contributor)
  • Sébastien Boutet (Contributor)
  • J. E. Koglin (Contributor)
  • Garth J. Williams (Contributor)
  • Aaron S. Brewster (Contributor)
  • Karol Nass (Contributor)
  • Johan Hattne (Contributor)
  • Sabine Botha (Contributor)
  • R. B. Doak (Contributor)
  • Robert L. Shoeman (Contributor)
  • D. P. Deponte (Contributor)
  • Hyun Woo Park (Contributor)
  • Brian A. Federici (Contributor)
  • Nicholas K. Sauter (Contributor)
  • Ilme Schlichting (Contributor)
  • David Eisenberg (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2014-08-13
Deposition Date:2014-07-17
Revision Date:2014-09-03#2014-09-24#2018-02-14
Molecular Weight:66602.04
Macromolecule Type:Protein
Residue Count:587
Atom Site Count:4659

It has long been known that toxins produced by Bacillus thuringiensis (Bt) are stored in the bacterial cells in crystalline form. Here we describe the structure determination of the Cry3A toxin found naturally crystallized within Bt cells. When whole Bt cells were streamed into an X-ray free-electron laser beam we found that scattering from other cell components did not obscure diffraction from the crystals. The resolution limits of the best diffraction images collected from cells were the same as from isolated crystals. The integrity of the cells at the moment of diffraction is unclear; however, given the short time (∼ 5 µs) between exiting the injector to intersecting with the X-ray beam, our result is a 2.9-Å-resolution structure of a crystalline protein as it exists in a living cell. The study suggests that authentic in vivo diffraction studies can produce atomic-level structural information.
Date made available2014

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