Lattice self-assemblies (LSAs), which mimic protein assemblies, were studied using a new nonlinear vibrational imaging technique called vibrational sum-frequency generation (VSFG) microscopy. This technique successfully mapped out the mesoscopic morphology, microscopic geometry, symmetry, and ultrafast dynamics of an LSA formed by β-cyclodextrin (β-CD) and sodium dodecyl sulfate (SDS). The spatial imaging also revealed correlations between these different physical properties. Such knowledge shed light on the functions and mechanical properties of LSAs. In this Feature Article, we briefly introduce the fundamental principles of the VSFG microscope and then discuss the in-depth molecular physics of the LSAs revealed by this imaging technique. The application of the VSFG microscope to the artificial LSAs also paved the way for an alternative approach to studying the structure-dynamic-function relationships of protein assemblies, which were essential for life and difficult to study because of their various and complicated interactions. We expect that the hyperspectral VSFG microscope could be broadly applied to many noncentrosymmetric soft materials.