EMatch: discovery of high resolution structural homologues of protein domains in intermediate resolution cryo-EM maps.
Cryo-EM has become an increasingly powerful technique for elucidating the structure, dynamics, and function of large flexible macromolecule assemblies that cannot be determined at atomic resolution. However, due to the relatively low resolution of cryo-EM data, a major challenge is to identify components of complexes appearing in cryo-EM maps. Here, we describe EMatch, a novel integrated approach for recognizing structural homologues of protein domains present in a 6-10 A resolution cryo-EM map and constructing a quasi-atomic structural model of their assembly. The method is highly efficient and has been successfully validated on various simulated data. The strength of the method is demonstrated by a domain assembly of an experimental cryo-EM map of native GroEL at 6 A resolution.
Lasker
Keren
K
School of Computer Science, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Israel. kerenl@post.tau.ac.il
Dror
Oranit
O
Shatsky
Maxim
M
Nussinov
Ruth
R
Wolfson
Haim J
HJ
D033962:Adaptor Protein Complex 2 / Q000737:chemistry / Q000648:ultrastructure; D000465:Algorithms; D018834:Chaperonin 60 / Q000737:chemistry / Q000648:ultrastructure; D019295:Computational Biology / Q000379:methods*; D020285:Cryoelectron Microscopy / Q000379:methods*; D030562:Databases, Protein; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D008958:Models, Molecular; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein; D014305:Triose-Phosphate Isomerase / Q000737:chemistry / Q000648:ultrastructure
D033962:Adaptor Protein Complex 2; D018834:Chaperonin 60; D045322:Photosynthetic Reaction Center Complex Proteins; D014305:Triose-Phosphate Isomerase