Electrokinetically actuated protein crystallization

Currently, x-ray crystallography is the primary experimental tool employed to understand how proteins fold and assemble into well-defined structures. These diffraction methods critically depend the ability to produce high-purity crystal samples, but conventional crystallization processes are inherently slow and challenging to control. Here we explore a fundamentally different electrokinetically-actuated approach to overcome these limitations. Instead of the conventional method involving increasing protein concentration throughout the entire bulk volume using evaporation, we employ electrokinetics to increase protein concentration to achieve supersaturated conditions favorable for crystallization within a very small localized zone inside a microchannel network.