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

  1. Author:
    Lasker, K.
    Dror, O.
    Shatsky, M.
    Nussinov, R.
    Wolfson, H. J.

  2. Author Address

    Tel Aviv Univ, Raymond & Beverly Sackler Fac Exact Sci, Sch Comp Sci, IL-69978 Tel Aviv, Israel. Tel Aviv Univ, Sackler Fac Med, Dept Human Genet & Mol Med, IL-69978 Tel Aviv, Israel. NCI, Frederick Canc Res & Dev Ctr, Ctr Canc Res Nanobiol Program, SAIC Frederick,Basic Res Program, Frederick, MD 21702 USA.;Lasker, K, Tel Aviv Univ, Raymond & Beverly Sackler Fac Exact Sci, Sch Comp Sci, IL-69978 Tel Aviv, Israel.;kerenl@post.tau.ac.il oranit@post.tau.ac.il maxshats@post.tau.ac.il ruthnu@post.tau.ac.il wolfson@post.tau.ac.il
    1. Year: 2007
    2. Date: Jan-Mar
  2. Journal: Ieee-Acm Transactions on Computational Biology and Bioinformatics
    1. 4
    2. 1
    3. Pages: 28-39
  4. Type of Article: Article
  5. ISSN: 1545-5963
  1. 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-EIM 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 angstrom 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 angstrom resolution.

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  1. View record in Web of Science®
  2. WOS: 000244645300005

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