Utilization of protein cages in biomimetic chemistry allows for the deposition of inorganic materials within an organic construct, controlling the size and amount of material deposited within a constrained reaction environment. Previously, protein cages such as viral capsids and ferritins have been used in the constrained synthesis of inorganic materials. The MrgA protein displays a high sequence homology to both bacterial DNA-protecting proteins (Dps) found in many bacterial genera and Ferritin-like proteins (Flp), which have been shown to functionally sequester and store iron in a biologically available form. Here we demonstrate recombinant production, purification and characterization of the MrgA protein and provide evidence that this protein self-assembles to form a multimeric complex. This complex demonstrates characteristics similar to that of ferritin-like proteins such as resistance to iron toxicity, iron incorporation, and resistance to thermal and chemical denaturation. The ability to deposit iron within the putative internal cavity of this protein cage will allow the MrgA complex to be utilized as a spatially constrained reaction vessel for nanomaterial synthesis of other inorganic materials. From a materials science perspective, it will be interesting to see if these organic/inorganic hybrid materials can be harnessed for catalysis, nanomagnetics, and other applications.