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In Vivo Crystallization of Three-Domain Cry Toxins

Department of Biotechnology, Lahore College for Women University, Lahore 54590, Pakistan
School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RH, UK
School of Biological Sciences, University of the Punjab, Quaid-i-Azam Campus, Lahore 54590, Pakistan
Authors to whom correspondence should be addressed.
Academic Editors: Juan Ferré and Baltasar Escriche
Toxins 2017, 9(3), 80;
Received: 13 January 2017 / Revised: 10 February 2017 / Accepted: 23 February 2017 / Published: 9 March 2017
(This article belongs to the Special Issue The Insecticidal Bacterial Toxins in Modern Agriculture)
PDF [798 KB, uploaded 9 March 2017]


Bacillus thuringiensis (Bt) is the most successful, environmentally-friendly, and intensively studied microbial insecticide. The major characteristic of Bt is the production of proteinaceous crystals containing toxins with specific activity against many pests including dipteran, lepidopteran, and coleopteran insects, as well as nematodes, protozoa, flukes, and mites. These crystals allow large quantities of the protein toxins to remain stable in the environment until ingested by a susceptible host. It has been previously established that 135 kDa Cry proteins have a crystallization domain at their C-terminal end. In the absence of this domain, Cry proteins often need helper proteins or other factors for crystallization. In this review, we classify the Cry proteins based on their requirements for crystallization. View Full-Text
Keywords: Bacillus thuringiensis; C terminal domain; helper protein Bacillus thuringiensis; C terminal domain; helper protein

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Adalat, R.; Saleem, F.; Crickmore, N.; Naz, S.; Shakoori, A.R. In Vivo Crystallization of Three-Domain Cry Toxins. Toxins 2017, 9, 80.

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