<italic>Fragon</italic>: rapid high‐resolution structure determination from ideal protein fragments.

Correctly positioning ideal protein fragments by molecular replacement presents an attractive method for obtaining preliminary phases when no template structure for molecular replacement is available. This has been exploited in several existing pipelines. This paper presents a new pipeline, named <italic>Fragon</italic>, in which fragments (ideal α‐helices or β‐strands) are placed using <italic>Phaser</italic> and the phases calculated from these coordinates are then improved by the density‐modification methods provided by <italic>ACORN</italic>. The reliable scoring algorithm provided by <italic>ACORN</italic> identifies success. In these cases, the resulting phases are usually of sufficient quality to enable automated model building of the entire structure. <italic>Fragon</italic> was evaluated against two test sets comprising mixed α/β folds and all‐β folds at resolutions between 1.0 and 1.7 Å. Success rates of 61% for the mixed α/β test set and 30% for the all‐β test set were achieved. In almost 70% of successful runs, fragment placement and density modification took less than 30 min on relatively modest four‐core desktop computers. In all successful runs the best set of phases enabled automated model building with <italic>ARP</italic>/<italic>wARP</italic> to complete the structure. [ABSTRACT FROM AUTHOR]