Less Is More: Structures of Difficult Targets with Minimal Constraints

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.
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Sprache:eng
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Carrier Proteins - chemistry
Glycoproteins - chemistry
Viral Proteins - chemistry
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container_title Structure (London)
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creator Lloyd, Neil R.
Wuttke, Deborah S.
description 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.
doi_str_mv 10.1016/j.str.2014.08.004
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subjects Carrier Proteins - chemistry
Glycoproteins - chemistry
Viral Proteins - chemistry
title Less Is More: Structures of Difficult Targets with Minimal Constraints
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