EMatch: Discovery of High Resolution Structural Homologues of Protein Domains in Intermediate Resolution Cryo-EM Maps
Issue No. 01 - January-March (2007 vol. 4)
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 Å 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 Å resolution.
Structural bioinformatics, intermediate resolution cryo-EM maps, 3D alignment of secondary structures, macromolecular assemblies, cyclic symmetry.
H. J. Wolfson, O. Dror, K. Lasker, R. Nussinov and M. Shatsky, "EMatch: Discovery of High Resolution Structural Homologues of Protein Domains in Intermediate Resolution Cryo-EM Maps," in IEEE/ACM Transactions on Computational Biology and Bioinformatics, vol. 4, no. , pp. 28-39, 2007.