Fatty acids (FAs) transport from lipid droplets (LDs) to mitochondria is essential for cellular survival under nutrient stress. It remains unclear whether amphipathic FAs can be directly transferred via LD–mitochondria membrane contact sites. The autophagy-related protein 2 (ATG2), a bridge-like lipid transfer protein, is critical for this process, yet how it mediates FA transport remains unresolved. Here, we examined the in situ architecture of ATG2 at LD–mitochondria contact sites using cryo-electron tomography (cryo-ET), a molecular-resolution imaging technique that preserves near-native cellular ultrastructure and molecular organization. This was complemented by correlative light and electron microscopy (CLEM) and cryo-focused ion beam (cryo-FIB) milling. Tethering ATG2 to the mitochondrial outer membrane revealed 20-nm bridging densities spanning LD-mitochondria contact sites. Ongoing work aims to resolve the architecture of wild-type ATG2 under starvation and compare it to its conformation under basal conditions, shedding light on the mechanism of FA transfer.