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It is critical to determine the binding mode between small molecule drugs and their protein targets for drug R&D. A comprehensive analysis of these interactions at both structural and physico-chemical levels could significantly deepen our understanding of protein functions and facilitate drug design & optimization. Structural biology techniques, including X-ray, cryo-electron microscopy (cryo-EM), nuclear magnetic resonance (NMR), etc., have been widely used in the determination of drug-binding modes. The high-resolution structures of protein-drug complexes could greatly benefit the optimization of drug structures in the early stage. However, protein structure analysis has consistently posed challenges in life science research, especially for membrane protein targets like G protein-coupled receptors (GPCRs) and ion channel proteins. It often consumes substantial time and resources on processes such as protein purification, screening for protein-drug complex crystallization, and data acquisition & processing.

An ideal approach is to identify protein-drug interaction modes within living cells.  This approach not only avoids high costs associated with structural studies, but also eliminate the possible false positives resulting from artificial conditions like high-salt buffers or saturated drugs.