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Chemical Crosslinking Mass Spectrometry (XL-MS) introduces covalent crosslinks between proteins or protein complexes, followed by mass spectrometry analysis to identify protein-protein interactions and elucidate macromolecular complex architectures. Core Principle: Bifunctional chemical crosslinkers (e.g., BS3, DSS, glutaraldehyde) react with specific amino acid residues (primarily lysine ε-amino groups, but also cysteine, tyrosine, etc.) on two proteins, forming a “molecular bridge”. After enzymatic digestion (typically trypsin), the crosslinked peptides are identified by high-resolution MS, revealing spatial proximity and interaction sites.