Complex nanoscale devices have great potential for use in the development of new materials, biosensors, electronics and pharmaceuticals. The potential to produce nanodevices is well supported by the numerous examples of self-assembling proteins found in nature. We are exploring self-assembling proteins as molecular building blocks to engineer nanocomponents. A promising candidate for engineering self-assembling nanocomponents is Lsr2. Lsr2 is a DNA binding protein present in mycobacterium and related actinobacteria that regulates gene expression. The key feature of Lsr2 is that it can be triggered to undergo self-assembly via proteolytic cleavage of the first N-terminal lysine residue. To better understand the self-assembling properties of Lsr2, a truncated form of this protein was prepared whereby the DNA binding site was deleted from the original sequence. In the absence of the DNA binding site, Nterm-Lsr2 provides us the opportunity of studying the triggerable oligomerisation site exclusively. In this manner we are able to explore the effects of pH, temperature, ionic strength and other factors on the oligomerisation of Nterm-Lsr2 and nanocomponent architecture. Herein, we report the first images (TEM) of oligomerised Nterm-Lsr2 of discrete sizes from isolated, SEC fractions. Furthermore, we report the effects of pH on the self-assembling potential of Nterm-Lsr2. Our results suggest that the oligomerisation of Nterm-Lsr2 can be controlled by more than one trigger. We envisage exploiting these triggers to develop switches capable of controlling the activation of self-assembly of Nterm-Lsr2 as well as manipulating the geometries of the nanoscale structures.