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The tracing of experimental electron maps in the field of protein crystallography is not a rate-limiting step for structure elucidation, but does represent the process that requires the most expertise and user time. This paper presents a method for automatically tracing the electron-density maps of proteins which can reliably generate a Cα trace for protein maps with data in the resolution range 1.5–4 Å. The number of Cα atoms placed and the precision of atom placement depends on the quality of the map, but even with poor maps (FOM ≃ 0.5) the algorithm can provide a significant saving in time over conventional methods of interpretation. The interpretation of six experimental maps is presented at different resolutions and levels of phase error; these show that data with an FOM of 0.7 or better can be entirely traced with no user intervention.

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