A crystal of the connector protein of a bacteriophage was irradiated by electrons during the observation in a transmission electron microscope at low temperature. The stress, resulting from the radiation damage, was eventually high enough to drive mass transport. The order quickly reemerged, before after longer irradiaton times the crystal was irreversibly damaged. Similar observations were made in a model experiment with a soap bubble crystal. After destroying a sufficient number of bubbles of a two-dimensional, hexagonally ordered raft of soap bubbles, the distorted crystal quickly reorderes by shifting the vacancies to the border of the crystal.
Thermal activation plays no role for the movement of the macroscopic bubbles.
These mass transport processes resemble very much the avalanches occuring in a pile of sand or snow, where slight distortions drive the system unstable. The subsequent 'mass slide' significantly lowers the energy, before the system locks into a metastable configuration again. However, in these latter systems no better degree of order is achieved by the mass transport. The stress-driven formation of order without diffusive mass transport might have particular consequences not only for the crystallization of proteins. It might be of particular relevance also for the epitaxial growth of crystalline material, important for thin layer technology and semiconductor fabrication.