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...

Full description

Saved in:
Bibliographic Details
Published inStructure (London) Vol. 22; no. 9; pp. 1223 - 1224
Main Authors Lloyd, Neil R., Wuttke, Deborah S.
Format Journal Article
LanguageEnglish
Published United States Elsevier Ltd 02.09.2014
Subjects
Online AccessGet full text

Cover

Loading…
More Information
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.
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