Posttranslational geranylgeranylation of Rab GTPases is catalyzed by Rab geranylgeranyltransferase (RabGGTase), which consists of a catalytic α/β heterodimer and an accessory Rab escort protein (REP). REP functions as a molecular chaperone that presents Rab proteins to the RabGGTase and after prenylation delivers them to their target membrane. Mutations in the REP-1 gene in humans lead to an X-chromosome-linked defect known as choroideremia, a progressive disease that inevitably culminates in complete blindness. Here we report in vitro assembly, purification, and crystallization of the monoprenylated Rab7GDP:REP-1 complex. X-Ray diffraction data for the REP-1:Rab7 complex were collected to 2.2-Å resolution at the ESRF. The crystals belong to the orthorhombic space group P2(1)2(1)2 with unit-cell parameters a=64.3 Å, b=105.3 Å, c=132.6 Å. Preliminary structural analysis revealed the presence of one complex in the asymmetric unit. To understand the conformational changes in Rab protein on complex formation we also crystallized the GDP-bound form of Rab7 that diffracted to at least 1.8 Å on the in-house X-ray source.