Here, we demonstrate an approach, binding-site purification of actives (B-SPA), that can indeed generate data not only at scale but also sampling chemical space suitably widely, and moreover at very low cost of synthesis. We have previously shown that crude reaction mixtures, from a single array of 2-component single-step reactions, yield eminently interpretable results of protein-ligand binding when using protein crystallography in combination with sensor-based affinity measurement (surface plasmon resonance, SPR). We now show that a more general synthetic approach remains effective, namely using array chemistry of diverse multi-step reactions that yield bespoke compounds in crude reaction mixtures. We exploit the fact that the binding site of the protein will extract the most potent species from complex mixtures of compounds, and that the effect can be observed by both biophysics or crystallography , now significantly more sensitively in the latter through ongoing developments in signal extraction. We previously completed a crystallographic fragment screen (PDB deposition ID: G_1002162) against the second bromodomain of the Pleckstrin Homology Domain-Interacting Protein (PHIP). This multidomain protein is involved in various cellular processes including cellular growth and mobility and has been implicated in aggressive cancers including BRAF-negative melanomas, breast and lung cancer ; nevertheless, the specific role of the second bromodomain (hereafter: PHIP(2)) is unknown.