Once the malaria parasite Plasmodium falciparum has invaded the human host erythrocyte it starts remodelling its new home immensely. A new trafficking apparatus is set up within the red blood cell, which is devoid of any organelles itsself. Nutrients are delivered from the outside of the cell to the parasite and proteins from within the parasite to the cytoplasm and surface of the host cell via this route. Both events are essential for the survival of the parasite. The latter event provides the parasite with the opportunity to escape the human immune response by transporting a number of proteins underneath and onto the red blood cell membrane. The major virulence factor Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) has to be displayed on elevated structures on the surface of the erythrocyte, so called knobs, in order to confer cytoadherence to various ligands on endothelia of different organs in the human host. This leads to occlusion of blood vessels and to the most severe symptoms in malaria patients (e.g. cerebral malaria). We have studied a number of exported proteins and will report on microscopical techniques we used in order to characterise these proteins including immunofluorescence assay, scanning electron microscopy, various transmission electron microscopy approaches (including cryo tomography) and atomic force microscopy. The deletion of one of the proteins presented results in dramatic alterations in morphology of organelles essential for protein transport to the surface of the infected red blood cell (so called Maurer’s clefts) and in actin cytoskeleton linkage. Other known Maurer’s clefts resident proteins localise to vesicular structures that appear to represent deformed Maurer’s clefts. We will report on possible functions of these proteins in PfEMP1 transport to and display on the surface of the infected red blood cell and Maurer’s cleft architecture.