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Publication Abstract from PubMed

For almost half a century, the structure of the full-length Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac has eluded researchers, since Bt-derived crystals were first characterized in 1965. Having finally solved this structure we report intriguing details of the lattice-based interactions between the toxic core of the protein and the protoxin domains. The structure provides concrete evidence for the function of the protoxin as an enhancer of native crystal packing and stability.

Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.,Evdokimov AG, Moshiri F, Sturman EJ, Rydel TJ, Zheng M, Seale JW, Franklin S Protein Sci. 2014 Nov;23(11):1491-7. doi: 10.1002/pro.2536. Epub 2014 Sep 2. PMID:25139047^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.