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@ARTICLE{Schrder:155679,
author = {Schröder, Gunnar and Levitt, Michael and Brunger, Axel T.},
title = {{D}eformable elastic network refinement for low-resolution
macromolecular crystallography},
journal = {Acta crystallographica / D},
volume = {70},
number = {9},
issn = {1399-0047},
address = {Copenhagen},
publisher = {Munksgaard},
reportid = {FZJ-2014-04732},
pages = {2241 - 2255},
year = {2014},
abstract = {Crystals of membrane proteins and protein complexes often
diffract to low resolution owing to their intrinsic
molecular flexibility, heterogeneity or the mosaic spread of
micro-domains. At low resolution, the building and
refinement of atomic models is a more challenging task. The
deformable elastic network (DEN) refinement method developed
previously has been instrumental in the determinion of
several structures at low resolution. Here, DEN refinement
is reviewed, recommendations for its optimal usage are
provided and its limitations are discussed. Representative
examples of the application of DEN refinement to challenging
cases of refinement at low resolution are presented. These
cases include soluble as well as membrane proteins
determined at limiting resolutions ranging from 3 to 7 Å.
Potential extensions of the DEN refinement technique and
future perspectives for the interpretation of low-resolution
crystal structures are also discussed.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000341819500001},
pubmed = {pmid:25195739},
doi = {10.1107/S1399004714016496},
url = {https://juser.fz-juelich.de/record/155679},
}