The Type III secretion system is a bacterial 'injectisome' which allows Gram-negative bacteria to shuttle virulence proteins directly into the host cells they infect. This macromolecular assembly consists of more than 20 different proteins put together to collectively span three biological membranes. The recent T3SS crystal structures of the major oligomeric inner membrane ring, the helical needle filament, needle tip protein, the associated ATPase, and outer membrane pilotin together with electron microscopy reconstructions have dramatically furthered our understanding of how this protein translocator functions. The crucial details that describe how these proteins assemble into this oligomeric complex will need a hybrid of structural methodologies including EM, crystallography, and NMR to clarify the intra- and inter-molecular interactions between different structural components of the apparatus.