ArticleNature communications2022
De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Interaction with theApplied and environmental microbiology · 2026Article
- Electron fourier ptychography for phase reconstruction.Scientific reports · 2025Article
- Intracellular protein crystallization in living insect cells.FEBS open bio · 2025Article
- Essential Role of Non-Conserved α4-HisProtein and peptide letters · 2025Article
- A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024Review
- Review
- Review
- A streamlined approach to structure elucidation using in cellulo crystallized recombinant proteins, InCellCryst.Nature communications · 2024Article
- Mutational analysis of the transmembrane α4-helix of Bacillus thuringiensis mosquito-larvicidal Cry4Aa toxin.Current microbiology · 2024Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Channel Formation in Cry Toxins: An Alphafold-2 Perspective.International journal of molecular sciences · 2023Article
- Toxic Determination of Cry11 Mutated Proteins Obtained Using Rational Design and Its Computational Analysis.International journal of molecular sciences · 2023Article
- Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced byFrontiers in insect science · 2023Review
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Authors and funding
63 authors.
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Abstract
Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan, respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo-grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable crystal packing motif is located within the protoxin rather than at the termini. The diversity of in vivo crystallization patterns suggests explanations for their varied levels of toxicity and rational approaches to improve these toxins for mosquito control.
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