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4QX0

Cry3A Toxin structure obtained by Serial Femtosecond Crystallography from in vivo grown crystals isolated from Bacillus thuringiensis and data processed with the cctbx.xfel software suite

Summary for 4QX0
Entry DOI10.2210/pdb4qx0/pdb
Related4QX1 4QX2 4QX3
DescriptorPesticidal crystal protein cry3Aa (2 entities 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 (2.8 Å)
Structure validation

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数据于2025-06-25公开中

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