Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 111, Issue 35, Pages 12769-12774Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1413456111
Keywords
XFEL; Cry3A insecticidal toxin; serial femtosecond crystallography
Categories
Funding
- National Center for Research Resources from the National Institutes of Health (NIH) [5P41RR015301-10]
- National Institute of General Medical Sciences from the National Institutes of Health (NIH) [8 P41 GM103403-10]
- US Department of Energy (DOE) [DE-AC02-06CH11357]
- DOE [DE-FC02-02ER63421]
- DOE Office of Basic Energy Sciences
- Linac Coherent Light Source Ultrafast Science Instruments project
- Keck Foundation [2843398]
- NIH [AG-029430, GM095887, GM102520, AI45817]
- National Science Foundation [MCB 0958111]
- Howard Hughes Medical Institute
- Max Planck Society
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0958111] Funding Source: National Science Foundation
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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 (similar to 5 mu s) between exiting the injector to intersecting with the X-ray beam, our result is a 2.9-angstrom-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.
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