Structural modeling of molecular assemblies lies at the heart of understanding molecular interactions and biological function. We present a method for docking protein molecules and elucidating native-like structures of protein dimers. Our method is based on geometric hashing to ensure the feasibility of searching the combined conformational space of dimeric structures. The search space is narrowed by focusing the sought rigid-body transformations around surface areas with evolutionary-conserved amino-acids. Recent analysis of protein assemblies reveals that many functional interfaces are significantly conserved throughout evolution. We test our method on a broad list of sixteen diverse protein dimers and compare the structures found to have lowest lRMSD to the known native dimeric structures to those reported by other groups. Our results show that focusing the search around evolutionary-conserved interfaces results in lower lRMSDs.