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Fragon

Fragon is a pipeline for molecular replacement in which fragments (ideal α-helices or β-strands) are placed using Phaser [1] and the phases calculated from these coordinates are improved by the density-modification methods provided by ACORN [2]. The reliable scoring algorithm provided by ACORN identifies successful cases and the resulting phases are usually of sufficient quality to enable automated model building of the entire structure.

References

If Fragon is useful please acknowledge the software that makes it possible:

  1. McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC & Read RJ. (2007). Phaser crystallographic software. J. Appl. Cryst. 40, 658-674. [https://doi.org/10.1107/S0021889807021206]

  2. Yao J-X, Woolfson MM, Wilson KS & Dodson EJ. (2005). A modified ACORN to solve protein structures at resolutions of 1.7 Å or better. Acta Cryst. D61, 1465-1475 [https://doi.org/10.1107/S090744490502576X]

and then the pipeline itself:

  1. Jenkins HT. (2018). Fragon: rapid high-resolution structure determination from ideal protein fragments. Acta Cryst. D74, 205–214. [https://doi.org/10.1107/S2059798318002292]

Thanks!

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