EMatch: discovery of high resolution structural homologues of protein domains in intermediate resolution cryo-EM maps.
IEEE/ACM Trans Comput Biol Bioinform
; 4(1): 28-39, 2007.
Article
in En
| MEDLINE
| ID: mdl-17277411
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 A resolution.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Image Processing, Computer-Assisted
/
Computational Biology
/
Cryoelectron Microscopy
Language:
En
Journal:
ACM Trans Comput Biol Bioinform
Journal subject:
BIOLOGIA
/
INFORMATICA MEDICA
Year:
2007
Document type:
Article
Affiliation country:
Israel
Publication country:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA