The primary parameters, secondary and tertiary structures and transmembrane regions of Bacillus thuringiensis toxins, Cry1Aa, Cry2Aa, Cry3Aa and Cry4Aa, were compared in bioinformatics. Considerable differences were found among the four toxins compared with each other in the primary structure, and many similarities were in the secondary structure and transmembrane regions. The structural diversity is smallest in domain I, domain II is the most divergent domain, and Cry2Aa is the most divergent member. The surface potentials over the four toxins were different. Those structural diversity and si...