Solution-stirring method improves crystal quality of human triosephosphate isomerase.

We examined the effect of a solution-stirring method on human triosephosphate isomerase crystallization. The crystals diffracted to more than 1.4 A resolution, whereas those obtained by the normal vapour-diffusion technique diffracted to 2.

Solution stirring initiates nucleation and improves the quality of adenosine deaminase crystals.

Crystals of bovine adenosine deaminase (ADA) grown over a two-week period in the presence of an inhibitor (ADA complex) were found to be of low quality for X-ray diffraction analysis. Furthermore, ADA incubated in the absence of an inhibitor (ADA native) did not form any crystals using conventional crystallization methods. A solution-stirring technique was used to obtain high-quality ADA complex and ADA native crystals.