Exploring the potential of a bioassembler for protein crystallization in space

Protein crystallization holds paramount significance in structural biology, serving as a pivotal technique for unveiling the three-dimensional (3D) architecture of proteins. While microgravity conditions in space offer distinct advantages for high-quality protein crystal growth by mitigating the influences of gravity and convection, the development of reliable techniques for protein crystallization in space with precise control over the crystallization process and its meticulous inspections remains a challenge. In this study, we present an innovative bioassembler-specifically, the 'Organ.Aut'-which we successfully employed to crystallize protein in space. The bioassembler 'Organ.Aut' produced highly ordered crystals diffracted to a true-atomic resolution of similar to 1 & Aring;. These data allowed for a detailed examination of atomic structures, enabling thorough structural comparisons with crystals grown on Earth. Our finding suggests that the bioassembler 'Organ.Aut' stands as a promising and viable option for advancing protein crystallization in space.