Unveiling Sugar Molecular Structures Through Galectin-10 Protein Crystals
A groundbreaking advance in the field of structural biology has emerged from the Institute of Science Tokyo, where researchers have developed an innovative, rapid, and purification-free technique for elucidating detailed three-dimensional structures of flexible sugar molecules. Sugars, or saccharides, which play far more complex and critical roles in biological systems than their common association with sweetness suggests, have long posed formidable challenges to structural characterization due to their inherent flexibility and dynamic conformations. This pioneering method leverages cell-free protein crystallization (CFPC) of galectin-10 (Gal-10), a sugar-binding lectin, to create molecular crystals capable of capturing and stabilizing sugar molecules, enabling unprecedented high-resolution analysis of their atomic arrangements through X-ray crystallography.
In living organisms, carbohydrates serve as crucial mediators of cell-cell communication, infection control, and tissue regeneration. They embellish cell surfaces, creating a dynamic molecular interface crucial for countless physiological processes. Decoding how these sugar molecules fold and interact with proteins is vital to understanding their biological functions. However, their flexible nature has historically thwarted efforts to obtain precise structural insights, as conventional crystallographic and spectroscopic techniques often falter when confronted with molecular heterogeneity and rapid conformational change.
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