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Structural biology explores the three-dimensional architecture of biologically significant molecules and macromolecules like carbohydrates, proteins, and nucleic acids. These molecules' functions are largely determined by their 3D shapes. By uncovering their atomic structures, researchers can better understand their mechanisms and how genetic mutations or deletions lead to specific diseases. Examining protein structures at the atomic level also enables the targeted design of small molecules to modify their function, offering promising therapeutic applications. The primary methods for determining macromolecular structures at atomic resolution are X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. In our department, these techniques help investigate proteins involved in immune responses, retroviral assembly, and cell-surface carbohydrate structures. Recently, additional methods like electrospray ionization mass spectrometry (ESI-MS) have emerged to analyze macromolecular structures that NMR or X-ray crystallography cannot resolve. Our team applies this technique to study nucleic acids and protein-nucleic acid complexes in retroviruses.