@article{oai:repo.qst.go.jp:00080142,
 author = {南畑, 孝介(東大院・工) and 塚本, 啓介(東大院・工) and 安達, 基泰 and 清水, 瑠美 and Masahiro, Mishina(東大院・工) and 長棟輝行(東大院・工) and Adachi, Motoyasu and Shimizu, Rumi},
 issue = {27},
 journal = {Chemical Communications},
 month = {Apr},
 note = {Protein crystals are important materials in X-ray crystallography to reveal the 3D structure of proteins but they are also attractive as a reaction vessel or template for nanomaterials; however, crystallizing protein is extremely difficult, hampering such utilization of protein crystals. We serendipitously discovered that streptavidin crystals form instantaneously upon mixing streptavidins with positively or negatively charged peptides at their C-termini. Hybrid crystals of streptavidin with charged oligo-peptides, oligo-DNA, and dendrimers were also obtained via interaction between the charged peptides on streptavidins and the small charged molecules. This technique uses simple electrostatic interaction between the charged peptides; therefore it should be applicable to many proteins, defying the stereotypes about protein crystallization and facilitating the use of protein crystals as functional materials.},
 pages = {3891--3894},
 title = {Genetically fused charged peptides induce rapid crystallization of protein.},
 volume = {56},
 year = {2020}
}