The capabilities of current protein structure prediction methods have been assessed from the outcome of a set of blind tests. In comparative modeling, many of the numerical methods did not perform as well as expected, although the resulting structures are still of great practical use. The new methods of fold identification ('threading') were partially successful, and show considerable promise for the future. Except for secondary structure data, results from traditional ab initio methods were poor. A second blind prediction experiment is underway, and progress in all areas is expected.