A pulsed diffusion technique for the growth of protein crystals for x-ray diffraction.

Abstract

Crystals of proteins suitable for X-ray diffraction have been grown using a method that combines dialysis (Zeppezauer et al., 1968) and relaxation (Salemme, 1972) techniques. This pulsed-diffusion method is useful for (a) eliminating unwanted amorphous precipitate, and (b) reducing the number of crystal nuclei which form and thus growing each individual crystal larger. The method is illustrated for glutamate-aspartate transaminase and thymidylate synthetase. Preliminary crystallographic data are reported for crystals of thymidylate synthetase.