Most research in contemporary molecular biology depends on an exact knowledge of protein structure and therefore on the availability of protein crystals, which are difficult to grow and often too imperfect for good structural resolution. Protein crystals grown in microgravity are often either better or worse than when grown on the ground, suggesting that optimal growth may depend on better control of convection and/or growth rate, so as to make either solute transport or interface kinetics the dominant process.
We recently attempted to develop such control by using new configurations and driving forces for protein crystallization. Our research to date has included new configurations for convectionless growth by vapor-transport, electrolysis and centrifugation. We are considering further exploration and exploitation of these three techniques to achieve optimal protein crystal quality. It is hoped that the development of these new growth techniques will expand the range of options available to protein crystallographers.
Although this project is currently dormant because of the demands of other projects, we are currently seeking collaborators, well versed in protein crystallization techniques, for possible future research. An extension of this project, the growth of inorganic crystals by centrifugation, is still active.

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