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A New Chemical Reactor for Protein Crystal Growth



David Travis Gallagher, C Stover, J Moses, D Charlton, E Steinberg, L Arnowitz


Current rapid advances in the genomic and biochemical sciences provide impetus for finding improved ways of crystallizing proteins for structure determination. A new dialysis-based reactor for protein crystal growth is described. The device utilizes motor-driven syringes to provide greater dynamic control of the growth conditions than is possible using conventional methods (e.g. hanging drops). The new reactor was tested in comparison with hanging drops, using the protein Rnase S. Multiple 2-day runs with both methods were conducted over a wide concentration range of the precipitant sodium chloride in a background of quarter-saturated ammonium sulfate with acetate buffer at pH 5. The results confirm (for both methods) that an optimum range of precipitant (55-60 percent of saturation) exists for producing large crystals, and show that the new hardware is at least equal in its effectiveness for crystallizing this protein to sizes useful for x-ray diffraction. Based on these results, it is likely that other more fragile proteins would benefit significantly from the greater control offered by the new device.
Biotechnology Progress


crystallization, dialysis, dynamic control, protein crystal growth, ribonuclease


Gallagher, D. , Stover, C. , Moses, J. , Charlton, D. , Steinberg, E. and Arnowitz, L. (2008), A New Chemical Reactor for Protein Crystal Growth, Biotechnology Progress (Accessed April 16, 2024)
Created October 16, 2008