4QX2 : Cry3A Toxin structure obtained by injecting Bacillus thuringiensis cells in an XFEL beam, collecting data by serial femtosecond crystallographic methods and processing data with the cctbx.xfel software suite

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

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.9
Classification:TOXIN
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
DOI:10.2210/pdb4qx2/pdb

Abstract:
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 availableAug 13 2014
PublisherRCSB-PDB

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