Adjustment of Protein Crystal Porosity for Biotemplating: Chemical and Protein Engineering Tools

摘要

Protein crystals, routinely prepared for the elucidation of protein 3D structures by X-ray crystallography, present an ordered and highly accurate 3D array of protein molecules. Inherent to the 3D arrangement of the protein molecules in the crystal is a complementary 3D array of voids made of interconnected cavities and exhibiting highly ordered porosity. Here we propose and demonstrate feasibility of using chemical and genetic tools to alter protein crystal packing by a series of modifications of targeted sites on protein's surface, enabling the generation of a series of protein crystal biotemplates, all originating from same parent protein.