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<i>Bacillus thuringiensis</i> (<i>Bt</i>) is a natural crystal-making bacterium. <i>Bt</i> diversified into many subspecies that have evolved to produce crystals of hundreds of pesticidal proteins with radically different structures. Their crystalline form ensures stability and controlled release of these major virulence factors. They are responsible for the toxicity and host specificity of <i>Bt</i>, explaining its worldwide use as a biological insecticide. Most research has been devoted to understanding the mechanisms of toxicity of these toxins while the features driving their crystallization have long remained elusive, essentially due to technical limitations. The evolution of methods in structural biology, pushing back the limits in size of amenable protein crystals now allows access to be gained to structural information hidden within natural crystals of such toxins. In this review, we present the main parameters that have been identified as key drivers of toxin crystallization in <i>Bt</i>, notably in the light of recent discoveries driven by structural biology studies. Then, we develop how the future evolution of structural biology will hopefully unveil new mechanisms of <i>Bt</i> toxin crystallization, opening the door to their hijacking with the aim of developing a versatile in vivo crystallization platform of high academic and industrial interest.