Axons and dendrites possess a distinctive arrangement of their cortical cytoskeleton known as the Membrane-associated Periodic Skeleton (MPS). The MPS is formed by actin rings arranged transversely to the axon and spaced every ~190 nm by α/β-spectrin tetramers. Since its discovery, research has primarily focused on its longitudinal organization, particularly in neuronal in vitro models. However, despite advances in identifying essential and accessory MPS components, it remains unclear how these elements are assembled within each segment, especially in transverse sections. To address this, we analyzed the distribution of βII-spectrin in mouse sciatic nerve axons (in situ) using 3D-STORM microscopy. We found that βII-spectrin is organized in clusters located mainly at the axonal perimeter, corresponding to the MPS. These clusters display regular spacing, maintaining a consistent distance, and aligned with the number of clusters per segment –that is proportional to perimeter length. Together, these findings indicate that the transverse organization of βII-spectrin in the peripheral nervous system is not only highly ordered but also adaptable, supporting its structural role in maintaining axonal integrity.