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The long and short of it : Distinct natural crystal packing strategies of Cry toxins from Bacillus thuringiensis

Best, Hannah L ; Williamson, Lainey J ; Cutts, Adam B ; Galchenkova, Marina ; Yefanov, Oleksandr ; Bryce-Sharron, Nicole ; Heath, Emily A ; de Wijn, Raphael ; Schubert, Robin and Munke, Anna LU orcid , et al. (2026) In Structure
Abstract

Bacillus thuringiensis (Bt) strains naturally produce pesticidal proteins as nanocrystalline inclusions that are extraordinarily stable in aqueous environments, but which dissolve selectively at specific pH conditions. These proteins have been used in agriculture for >50 years and are critical to global food security. The majority of previously determined Bt Cry protein structures lack the extended C-terminal "crystallization domain," which is thought to stabilize crystal packing and control selective solubility in insect targets, often via manipulation of disulfide bridges. It has also recently been shown to influence toxicity and target specificity. Here, we use serial femtosecond crystallography (SFX) to determine high-resolution... (More)

Bacillus thuringiensis (Bt) strains naturally produce pesticidal proteins as nanocrystalline inclusions that are extraordinarily stable in aqueous environments, but which dissolve selectively at specific pH conditions. These proteins have been used in agriculture for >50 years and are critical to global food security. The majority of previously determined Bt Cry protein structures lack the extended C-terminal "crystallization domain," which is thought to stabilize crystal packing and control selective solubility in insect targets, often via manipulation of disulfide bridges. It has also recently been shown to influence toxicity and target specificity. Here, we use serial femtosecond crystallography (SFX) to determine high-resolution full-length native structures of Cry1Ca18 (1.65 Å) and Cry8Ba2 (2.27 Å) in their natural nanocrystalline state. Differences in cysteine content (19 versus 4 residues) reveal distinct in vivo crystal-stabilization strategies. Understanding Bt toxin domain architecture and natural crystal formation is essential for improving biopesticide design and advancing agricultural genetic engineering.

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publishing date
type
Contribution to journal
publication status
epub
in
Structure
publisher
Cell Press
external identifiers
  • pmid:41734756
  • scopus:105033716179
ISSN
0969-2126
DOI
10.1016/j.str.2026.01.014
language
English
LU publication?
no
additional info
Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.
id
bf94aefa-6c5f-4e8c-9d53-15af9072da0e
date added to LUP
2026-02-27 15:48:51
date last changed
2026-04-10 04:00:31
@article{bf94aefa-6c5f-4e8c-9d53-15af9072da0e,
  abstract     = {{<p>Bacillus thuringiensis (Bt) strains naturally produce pesticidal proteins as nanocrystalline inclusions that are extraordinarily stable in aqueous environments, but which dissolve selectively at specific pH conditions. These proteins have been used in agriculture for &gt;50 years and are critical to global food security. The majority of previously determined Bt Cry protein structures lack the extended C-terminal "crystallization domain," which is thought to stabilize crystal packing and control selective solubility in insect targets, often via manipulation of disulfide bridges. It has also recently been shown to influence toxicity and target specificity. Here, we use serial femtosecond crystallography (SFX) to determine high-resolution full-length native structures of Cry1Ca18 (1.65 Å) and Cry8Ba2 (2.27 Å) in their natural nanocrystalline state. Differences in cysteine content (19 versus 4 residues) reveal distinct in vivo crystal-stabilization strategies. Understanding Bt toxin domain architecture and natural crystal formation is essential for improving biopesticide design and advancing agricultural genetic engineering.</p>}},
  author       = {{Best, Hannah L and Williamson, Lainey J and Cutts, Adam B and Galchenkova, Marina and Yefanov, Oleksandr and Bryce-Sharron, Nicole and Heath, Emily A and de Wijn, Raphael and Schubert, Robin and Munke, Anna and Henkel, Alessandra and Klopprogge, Bjarne and Scheer, T Emilie S and Kremling, Viviane and Awel, Salah and Pena, Gisel and Knoska, Juraj and Keloth, Anusha and Maracke, Julia and Letrun, Romain and Sobolev, Egor and Bielecki, Johan and Melo, Diogo and Kantamneni, Sravya and Doerner, Katerina and Kloos, Marco and Schulz, Joachim and Xavier, P Lourdu and Lauffer, Marius and Villanueva, Maite and Caballero, Primitivo and Waller-Evans, Helen and Lloyd-Evans, Emyr and Uetrecht, Charlotte and Bean, Richard and Chapman, Henry N and Crickmore, Neil and Rizkallah, Pierre J and Berry, Colin and Oberthür, Dominik}},
  issn         = {{0969-2126}},
  language     = {{eng}},
  month        = {{02}},
  publisher    = {{Cell Press}},
  series       = {{Structure}},
  title        = {{The long and short of it : Distinct natural crystal packing strategies of Cry toxins from <i>Bacillus thuringiensis</i>}},
  url          = {{http://dx.doi.org/10.1016/j.str.2026.01.014}},
  doi          = {{10.1016/j.str.2026.01.014}},
  year         = {{2026}},
}