The high-resolution prediction of protein-protein docking can now create structures with atomic-level accuracy. This progress arises from both improvements in the rapid sampling of conformations and increased accuracy of binding free energy calculations. Consequently, the quality of models submitted to the blind prediction challenge CAPRI (Critical Assessment of PRedicted Interactions) has steadily increased, including complexes predicted from homology structures of one binding partner and complexes with atomic accuracy at the interface. By exploiting experimental information, docking has created model structures for real applications, even when confronted with challenges such as moving backbones and uncertain monomer structures. Work remains to be done in docking large or flexible proteins, ranking models consistently, and producing models accurate enough to allow computational design of higher affinities or specificities.