Use LFS to determine more complex structures

Achieve higher success rates with the new Ligand-Friendly Screen, optimised for compound binding studies.

The Ligand-Friendly Screen (LFS)1 has been one of the two primary coarse screens of the Structural Genomics Consortium (SGC) in Oxford since 2004; at last count, it had produced 190 novel structures over 10 years.

The screen was developed in the Protein Crystallography group of Prof. Frank von Delft, which also developed one our most successful screens of 2017: The BCS screen2. The LFS was designed by Prof. Janet Newman (who has since set up the Collaborative Crystallisation Centre, CSIRO, Australia) andFrank von Delft  as a modification of Prof. Newman's popular PACT3: it screens combinations of PEG (1K to 6K), salts and buffers at near-physiological pH in a semi-systematic manner.

The LFS is designed to provide crystals that are directly usable for compound binding studies:

  • Identify more tight-binding ligands, as it contains no components that are likely to bind at protein-ligand interaction sites. LFS additives will not competitively inhibit the binding of lead-discovery screen compounds to your protein.
  • Increases the chance that you are studying the active, functionally-relevant form of your protein by using only near-physiological pH conditions.
  • More hits for rarely-crystallising proteins. The semi-systematic format of the screen results in a relatively high level of internal redundancy, providing multiple trials of similar conditions - an important factor in these difficult cases.
  • Increased hit rate when cocrystallising a protein with a range of related ligands that affect the optimal conditions for crystal growth, as the semi-systematic format means that closely-related conditions are efficiently screened.

The LFS has been used at the SGC for several years already, and is described in Ng, J.T, 20151. Its use as one of their standard screens has resulted in numerous successful crystallisations and subsequent publications. Examples of protein structures solved with conditions found in LFS include CLK3 in complex with a new inhibitor chemotype4 (right) and Haspin in complex with a range of halo-aromatic inhibitors5(top).

The LFS together with the BCS screen (also from the SGC) represent a powerful combination for successful structure solution and compound-binding studies. Use both to maximise your crystallisation success rate.
  1. Ng, J.T. et al. Acta Cryst. D72: 224-235 (2015).
  2. Chaikuad, A. Knapp, S. and von Delft, F. Acta Cryst F71: 1627-1639 (2015).
  3. Newman, J. et al.Acta Cryst. D61: 1426–1431 (2005).
  4. Walter, A. et al. PLoS One13: 96761 (2018).
  5. Heroven et al. Angew. Chem. Int. Ed. Engl. 57: 7220-7224 (2018).


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