EMatch: Discovery of high resolution structural homologues of protein domains in intermediate resolution Cryo-EM maps

Keren Lasker, Oranit Dror, Maxim Shatsky, Ruth Nussinov, Haim J. Wolfson

Research output: Contribution to journalArticlepeer-review

Abstract

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 Å resolution.

Original languageEnglish
Pages (from-to)28-39
Number of pages12
JournalIEEE/ACM Transactions on Computational Biology and Bioinformatics
Volume4
Issue number1
DOIs
StatePublished - Jan 2007

Keywords

  • 3D alignment of secondary structures
  • Cyclic symmetry
  • Intermediate resolution cryo-EM maps
  • Macromolecular assemblies
  • Structural bioinformatics

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