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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Published in | Structure (London) Vol. 22; no. 9; pp. 1223 - 1224 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Ltd
02.09.2014
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Commentary-2 ObjectType-Feature-3 content type line 23 |
ISSN: | 0969-2126 1878-4186 |
DOI: | 10.1016/j.str.2014.08.004 |