Integration of cryo-EM with atomic and protein-protein interaction data.
Cryoelectron microscopy (cryo-EM) is an increasingly popular method to elucidate the structures of macromolecular complexes. However, in many applications the resolution of cryo-EM densities is limited to the low or intermediate resolution regime, that is, (10Å)(-1) or worse. Therefore, unambiguous molecular interpretation of cryo-EM densities requires efficient use of additional information, such as atomic structures of related subunits and protein-protein interaction data. Here, we describe how information from different sources can be combined to determine the approximate molecular architecture of complexes. Molecular dynamics based flexible fitting protocols allow subsequent refinement of the atomistic models.
Förster
Friedrich
F
Max-Planck Institute of Biochemistry, Department of Structural Biology, Martinsried, Germany.
Villa
Elizabeth
E
D000595:Amino Acid Sequence; D020285:Cryoelectron Microscopy / Q000379:methods*; D046911:Macromolecular Substances / Q000032:analysis; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000648:ultrastructure; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D021122:Protein Subunits / Q000737:chemistry*; D011506:Proteins / Q000032:analysis; D016415:Sequence Alignment
D046911:Macromolecular Substances; D021122:Protein Subunits; D011506:Proteins; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease