Abstract

X-ray crystallography plays a pivotal role in drug discovery by providing detailed insights into the molecular interactions between drug candidates and their biological targets. This abstract highlights the significance of X-ray crystallography in elucidating the three-dimensional structures of protein-ligand complexes, which are crucial for understanding binding affinities and mechanisms of action. By revealing the atomic details of these interactions, researchers can identify key binding sites, optimize lead compounds, and design more effective therapeutics. Recent advancements in crystallographic techniques, such as high-throughput screening and the use of cryo-electron microscopy, have further accelerated the process of structure-based drug design. This review emphasizes how X-ray crystallography not only aids in the rational design of new drugs but also contributes to the identification of novel targets, ultimately enhancing the efficiency and success rates of drug development. Through the integration of structural data with computational modeling and bioinformatics, X-ray crystallography continues to be an indispensable tool in the evolving landscape of drug discovery.