Self-Assembly of Protein Crystals with Different Crystal Structures Using Tobacco Mosaic Virus Coat Protein as a Building Block

• DOI: 10.1021/acsnano.7b08316
• Publication Date: 2018-01-19T19:47:51Z
• Authors: Jianting Zhang; Xiao Wang; Kun Zhou; Gang Chen; Qiangbin Wang
• Keywords: Triclinic crystal system; Protein crystallization; Crystal (programming language)

In this work, a typical cylinder-shaped tobacco mosaic virus coat protein (TMVCP) is employed as an anisotropic building block to assemble into triclinic and hexagonal close-packed (HCP) crystals by introducing cysteine residues at the 1 3 sites four histidine C-terminal, respectively. The engineered functional groups of in TMVCP self-assembly conditions determine thermodynamics kinetics process for forming different crystal structures. results show that TMVCPs are thermodynamically driven form due formation disulfide bonds between neighboring TMVCPs. On other hand, HCP kinetically directed strong metal-histidine chelation. This work not only greatly expands fabricating promising nanomaterials but also represents approach adjusting structures tuning during crystallization.