@article{
 id = {68f71552-0a1b-3000-a723-c7a2fa353a36},
 title = {EM-fold: De novo folding of alpha-helical proteins guided by intermediate-resolution electron microscopy density maps.},
 type = {article},
 year = {2009},
 identifiers = {[object Object]},
 keywords = {Adenoviruses,Algorithms,Amino Acid,Amino Acid Sequence,Animals,Cattle,Chemical,Computational Biology,Computer Simulation,Cryoelectron Microscopy,Crystallography,Databases,Electron,Human,Human: chemistry,Human: ultrastructure,Humans,Microscopy,Models,Molecular,Molecular Sequence Data,Monte Carlo Method,Protein,Protein Conformation,Protein Folding,Protein Structure,Proteins,Proteins: chemistry,ROC Curve,Rhodopsin,Rhodopsin: chemistry,Rhodopsin: ultrastructure,Secondary,Sequence Homology,Software,X-Ray},
 created = {2010-08-22T22:09:01.000Z},
 pages = {990-1003},
 volume = {17},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/19604479},
 month = {7},
 file_attached = {true},
 profile_id = {ac6eb1b6-cd33-307e-a16e-bbe5db09e730},
 last_modified = {2014-03-25T19:42:56.000Z},
 read = {true},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 citation_key = {Lindert2009},
 client_data = {"desktop_id":"d8a8ed2b-f228-460a-ba9e-c5e4e5950edd"},
 abstract = {In medium-resolution (7-10 A) cryo-electron microscopy (cryo-EM) density maps, alpha helices can be identified as density rods whereas beta-strand or loop regions are not as easily discerned. We are proposing a computational protein structure prediction algorithm "EM-Fold" that resolves the density rod connectivity ambiguity by placing predicted alpha helices into the density rods and adding missing backbone coordinates in loop regions. In a benchmark of 11 mainly alpha-helical proteins of known structure a native-like model is identified in eight cases (rmsd 3.9-7.9 A). The three failures can be attributed to inaccuracies in the secondary structure prediction step that precedes EM-Fold. EM-Fold has been applied to the approximately 6 A resolution cryo-EM density map of protein IIIa from human adenovirus. We report the first topological model for the alpha-helical 400 residue N-terminal region of protein IIIa. EM-Fold also has the potential to interpret medium-resolution density maps in X-ray crystallography.},
 bibtype = {article},
 author = {Lindert, Steffen and Staritzbichler, René and Wötzel, Nils and Karakaş, Mert and Stewart, Phoebe L. and Meiler, Jens},
 journal = {Structure (London, England : 1993)},
 number = {7}
}

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