The Commander complex is a conserved regulator of intracellular trafficking. This ancient complex consists of 15 core components as well as a number of associated proteins that can be sub-divided into 3 categories. Commander can be further divided into two sub-assemblies called the Commd/CCDC22/CCDC93 (CCC) complex, and the trimeric Retriever complex with similarity to the endosomal Retromer trafficking machinery. The structure, mechanism and function of Commander remains largely elusive. In this work I have followed on from our previous investigation of individual Commd proteins (Healy et.al, 2018), by reconstituting the ten core Commd proteins using co-expression and affinity purification. The successful reconstitution of this complex using a polycistronic E. coli vector has allowed for the identification of two distinct subcomplexes of the Commd family, a result supported by mass spectrometry conducted in eHap cells. Moreover, we have successfully crystallised and resolved a ~3.3 Å structure of one of these subcomplexes, which reveals an intimately assembled hetero-tetramer, primarily mediated through the conserved C-terminal COMM domains of the four proteins. Modelling based on this sub-complex structure begins to suggest how the entire family of ten Commd proteins may associate to form a functional decameric assembly. Finally, in collaboration with the Tham laboratories we have identified a highly specific camelid-derived nanobody that we have used to isolate the Commander complex from HeLa cells. Taken together this work provides significant insights into how the highly conserved Commd proteins are functionally assembled.