Experimental information from small angle X-ray scattering (SAXS) is conjugated with nuclear magnetic resonance (NMR) spectroscopy data for the improvement of protein structure determination, particularly for flexible, multidomain or intrinsically disordered proteins. Individually, each of these techniques presents capabilities and limitations: NMR excels in local information, providing atomic resolution, but is limited by protein size, whereas SAXS yields a global envelope of the protein with lower resolution, but revealing domain positions. Different conjugation methodologies use the complementarity of both techniques’ independent constraints to achieve comprehensive protein structure determination and resolve dynamics at a moderate computational expense.

来自小角度X射线散射（SAXS）的实验信息与核磁共振（NMR）光谱数据相结合，以改善蛋白质结构的确定，尤其是对于柔性，多域或固有无序蛋白质。单独地，这些技术中的每一种都具有功能和局限性：NMR在提供原子分辨率方面在本地信息方面表现出色，但是受蛋白质大小的限制，而SAXS却产生了分辨率较低但揭示结构域位置的蛋白质全局包膜。不同的共轭方法使用这两种技术的独立约束条件的互补性来实现全面的蛋白质结构确定并以适度的计算费用解决动力学问题。