• Identify more tight-binding ligands, as it contains no components that are likely to bind at protein-ligand interaction sites.
• Near physiological pH conditions ensure you are studying the active form of your protein.
• More hits for rarely-crystallising proteins. The semi-systematic format of the screen provides multiple trials of similar conditions - an important factor for difficult cases.
• Increased hit rate for ligand co-crystallisations – the semi-systematic format efficiently screens around related conditions when complex formation alters crystallisation conditions.
• In use at the SGC for more than 10 years, crystals grown in the screen conditions have resulted in 190 structures so far, including those of Haspin¹ and CLK3² in recent publications.

The LFS is described in Ng, J. T. et al, 2015¹. Developed at the SGC, Oxford by the same group who created the successful BCS screen, launched last year and based on the popular PACT screen² created by Janet Newman at the Collaborative Crystallisation Centre, CSIRO.

References

1. Walter, A. et al. PLoS One13: 96761 (2018).
2. Heroven et al. Angew. Chem. Int. Ed. Engl. 57: 7220-7224 (2018).
3. Ng, J.T. et al. Acta Cryst. D72: 224-235 (2015).
4. Newman, J. et al.Acta Cryst. D61: 1426–1431 (2005).