In this project, the protein Malate Dehydrogenase was expressed and purified prior to the crosslinking analysis. Multiple crosslinkers of varying spacer lengths were applied to evaluate how its subunits are arranged. To determine if crosslinking occurred, a technique called SDS-Page was used, which separates proteins on a gel based on size. Successful crosslinking was indicated by larger protein bands representing two or more MDH units linked together. Crosslinking products were further confirmed by Western blot analysis, a technique that uses antibodies that specifically react with MDH to verify protein identity. Overall, these experiments helped to evaluate how efficiently MDH forms complexes and provided insight into its structure and interactions.