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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

Summary for 4QX2
Entry DOI10.2210/pdb4qx2/pdb
Related4QX0 4QX1 4QX3
DescriptorPesticidal crystal protein cry3Aa (1 entity in total)
Functional Keywordsin vivo crystals, microcrystals, serial femtosecond crystallography, sfx, lcls, x-ray free-electron laser, insecticidal toxin, toxin
Biological sourceBacillus thuringiensis serovar tenebrionis
Total number of polymer chains1
Total formula weight66602.04
Authors
Primary citationSawaya, M.R.,Cascio, D.,Gingery, M.,Rodriguez, J.,Goldschmidt, L.,Colletier, J.P.,Messerschmidt, M.M.,Boutet, S.,Koglin, J.E.,Williams, G.J.,Brewster, A.S.,Nass, K.,Hattne, J.,Botha, S.,Doak, R.B.,Shoeman, R.L.,DePonte, D.P.,Park, H.W.,Federici, B.A.,Sauter, N.K.,Schlichting, I.,Eisenberg, D.S.
Protein crystal structure obtained at 2.9 angstrom resolution from injecting bacterial cells into an X-ray free-electron laser beam.
Proc.Natl.Acad.Sci.USA, 111:12769-12774, 2014
Cited by
PubMed 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.
PubMed: 25136092
DOI: 10.1073/pnas.1413456111
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

226707

數據於2024-10-30公開中

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