Six protein-protein complexes and two homodimeric proteins involved in a variety of biological processes were offered as targets to CAPRI by crystallographers in Rounds 6-12. CAPRI predictor groups had to predict their structure by docking the free proteins, which they did with a degree of success that depended largely on the amplitude of the conformation changes. In one case at least, the prediction pointed to alternative possibilities of interactions in the crystal of a complex, showing that docking methods have value even when there is an experimental structure. 2007 Wiley-Liss, Inc.