Crystallising proteins, required for structure determination by X-ray diffraction, is a difficult and labour-intensive task. One of the many challenges facing the protein crystallographer is growing crystals of sufficient size and quality to successfully determine the protein’s structure (this typically requires crystals of around 100-300 3m).
For structure based drug design a further challenge is being able to generate a sustainable crystal system able to produce liganded structures iteratively to support
Microseeding, where small crystals are crushed and suspended in a slurry of crystallisation buffer to produce new nucleation sites, is a recognised technique to improve crystal quality as well as promote the growth of larger, single crystals. However, it requires experimentation with varying concentrations of solutions to achieve successful results.
The mosquito liquid handler (TTP Labtech) is ideally suited to automating the complex set-ups required for microseeding due to its precise handling of extremely low volumes of even viscous solutions, and its ability to perform multiple aspirations and dispenses with each pipette.