A Crystallographic-Based Fragment Screen Against Human BRD4 Bromodomain 1
Poster Oct 17, 2012
Hubbard P, Ritchie A, Hughes S, Lipkin M, Blackaby W & MacLeod A
Given that DMSO is a well known competitor of compound binding in human BRD4 bromodomain 1, we initially solved the crystal structure of this protein soaked in the presence of DMSO. Confirming that DMSO binds to the acetyllysine binding site, we commenced the fragment screen using ethanol as the compound solvent, allowing solvent to evaporate before solutions for protein crystal soaks were prepared. Fragments were batched into groups of three based on shape diversity and chemical compatibility, and datasets from soaked crystals that spanned the entire fragment library were collected using in-house X-ray diffraction equipment.
This poster presents a summary of the results, demonstrating how Biofocus’s structural biology capabilities complement their range of fragment screening services.
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