Résumé : The secretion apparatus known as the needle complex (NC) from the bacterium Shigella flexneri was studied by single particle electron microscopy. The isolated intact NC appears in projection to be composed of a basal body consisting of seven rings and a protruding needle appendage. A comparison of averaged projections of the intact NC and its fragments revealed the organization of the NC into several major subcomplexes. One of these lacks an inner membrane ring of the basal body but still presents the needle appendage attached to four upper rings. The position of the needle appendage within these rings is variable, suggesting that the dissociated component is necessary for stabilizing the needle appendage. Averaged images of the subcomplex lacking the inner membrane basal rings show a thicker extension at the base of the needle appendage, called the socket. This socket was also found to be present in images of the basal body fragment isolated from mutants lacking the mxiH and mxiI genes. This suggests that the socket is not composed of MxiH and MxiI subunits, which form the needle appendage. A symmetry analysis of the basal body top view projections indicated that a peripheral protein component of the inner membrane ring is present in a ring with 24 copies, in contrast to the Salmonella typhimurium NC. A model is presented in which the NC is only associated to the outer- and inner-membranes with its first and seventh ring, respectively.