The membrane structural biologist seeks to understand how membrane proteins function at a molecular level. One of the most direct ways of accomplishing this requires knowing the structure of the protein, ideally at atomic resolution. To date, this can only be done by the method of macromolecular crystallography. Integral to the method is the need for three-dimensional crystals of diffraction quality and their production represents a major rate-limiting step in the overall process of structure determination. The in meso method is a novel approach for crystallizing membrane proteins. It makes use of lipidic mesophases, the cubic phase in particular. A mechanism for how the method works has been proposed. In this study, we set out to test one aspect of the hypothesis which posits that the protein migrates from the bulk mesophase reservoir to the face of the crystal by way of a lamellar conduit. Using a sub-micrometer-sized X-ray beam the interface between a growing membrane protein crystal and the bulk cubic phase was interrogated with micrometer spatial resolution. Characteristic diffraction from the lamellar phase was observed at the interface as expected. This result supports the proposal that the protein uses a lamellar portal on its way from the bulk mesophase up and into the face of the crystal.