| Structural highlights
Function
YP067_YEAST
Publication Abstract from PubMed
We show here that computer game players can build high-quality crystal structures. Introduction of a new feature into the computer game Foldit allows players to build and real-space refine structures into electron density maps. To assess the usefulness of this feature, we held a crystallographic model-building competition between trained crystallographers, undergraduate students, Foldit players and automatic model-building algorithms. After removal of disordered residues, a team of Foldit players achieved the most accurate structure. Analysing the target protein of the competition, YPL067C, uncovered a new family of histidine triad proteins apparently involved in the prevention of amyloid toxicity. From this study, we conclude that crystallographers can utilize crowdsourcing to interpret electron density information and to produce structure solutions of the highest quality.
Determining crystal structures through crowdsourcing and coursework.,Horowitz S, Koepnick B, Martin R, Tymieniecki A, Winburn AA, Cooper S, Flatten J, Rogawski DS, Koropatkin NM, Hailu TT, Jain N, Koldewey P, Ahlstrom LS, Chapman MR, Sikkema AP, Skiba MA, Maloney FP, Beinlich FR, Popovic Z, Baker D, Khatib F, Bardwell JC Nat Commun. 2016 Sep 16;7:12549. doi: 10.1038/ncomms12549. PMID:27633552[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Horowitz S, Koepnick B, Martin R, Tymieniecki A, Winburn AA, Cooper S, Flatten J, Rogawski DS, Koropatkin NM, Hailu TT, Jain N, Koldewey P, Ahlstrom LS, Chapman MR, Sikkema AP, Skiba MA, Maloney FP, Beinlich FR, Popovic Z, Baker D, Khatib F, Bardwell JC. Determining crystal structures through crowdsourcing and coursework. Nat Commun. 2016 Sep 16;7:12549. doi: 10.1038/ncomms12549. PMID:27633552 doi:http://dx.doi.org/10.1038/ncomms12549
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