Less Is More: Structures of Difficult Targets with Minimal Constraints

By merging recent experimental and computational methodology advances, resolution-adapted structural recombination Rosetta has emerged as a powerful strategy for solving the structure of traditionally challenging targets. In this issue of Structure, Sgourakis and colleagues solve the structure of on...

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Veröffentlicht in:Structure (London) 2014-09, Vol.22 (9), p.1223-1224
Hauptverfasser: Lloyd, Neil R., Wuttke, Deborah S.
Format: Artikel
Sprache:eng
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Zusammenfassung:By merging recent experimental and computational methodology advances, resolution-adapted structural recombination Rosetta has emerged as a powerful strategy for solving the structure of traditionally challenging targets. In this issue of Structure, Sgourakis and colleagues solve the structure of one such target, the immunoevasin protein m04, using this approach. By merging recent experimental and computational methodology advances, resolution-adapted structural recombination Rosetta has emerged as a powerful strategy for solving the structure of traditionally challenging targets. In this issue of Structure, Sgourakis and colleagues solve the structure of one such target, the immunoevasin protein m04, using this approach.
ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2014.08.004