Abstract
Bacillus thuringiensis (or Bt) is commonly used as a biological pesticide; alternatively, the Cry toxin may be extracted and used as a pesticide. It occurs naturally in the gut of caterpillars of various types of moths and butterflies, as well as on the dark surfaces of plants. Bt crystals, sometimes referred to as insecticidal crystal proteins (ICP), are protein crystals formed during sporulation in some Bt strains. Bt produces proteins that aggregate to form a crystal. It is important to understand the mechanism of endotoxin binding or interaction with the host for the commercialization. Here, we aimed to construct computer-aided molecular model of bacterial endotoxin based comparative homology modeling, in order study the sequence in structural context and to analyze domains of the protein.