Open AccessDeformable elastic network refinement for low‐resolution macromolecular crystallography
Author(s) -
Schröder Gunnar F.,
Levitt Michael,
Brunger Axel T.
Publication year - 2014
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s1399004714016496
Subject(s) - resolution (logic) , limiting , flexibility (engineering) , low resolution , computer science , interpretation (philosophy) , algorithm , high resolution , crystallography , biological system , materials science , artificial intelligence , chemistry , mathematics , biology , mechanical engineering , geology , engineering , statistics , remote sensing , programming language
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.