Hierarchical self-assembly and crystallization with long-range ordered spatial arrangement is ubiquitous in nature and plays an essential role in the regulation of structures and biological functions. Proteins are polypeptide chains that can properly fold into particular 3D shapes via intramolecular noncovalent interactions, which can be devoted to the understanding of hierarchical self-assembly and crystallization of biomolecules, due to the protein features of conformational heterogeneity, flexibility, and complexity. Protein crystallization in living cells is more surprising as a native assembly process than in vitro, offering exciting new possibilities for the design and fabrication of bionic functional systems with long-range alignment of proteins.

Our work focus on the systematic investigation of the intracellular processes involved in crystal formation, how the crystals grow within cells and what controls their size and shape, how the morphology and properties of cells changes, opening in cellulo crystallization into a widely applicable field.