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TitleSeeing GroEL at 6 A resolution by single particle electron cryomicroscopy.
Journal, issue, pagesStructure, Vol. 12, Issue 7, Page 1129-1136, Year 2004
Publish dateFeb 9, 2005
AuthorsSteven J Ludtke / Dong-Hua Chen / Jiu-Li Song / David T Chuang / Wah Chiu /
PubMed AbstractWe present a reconstruction of native GroEL by electron cryomicroscopy (cryo-EM) and single particle analysis at 6 A resolution. alpha helices are clearly visible and beta sheet density is also ...We present a reconstruction of native GroEL by electron cryomicroscopy (cryo-EM) and single particle analysis at 6 A resolution. alpha helices are clearly visible and beta sheet density is also visible at this resolution. While the overall conformation of this structure is quite consistent with the published X-ray data, a measurable shift in the positions of three alpha helices in the intermediate domain is observed, not consistent with any of the 7 monomeric structures in the Protein Data Bank model (1OEL). In addition, there is evidence for slight rearrangement or flexibility in parts of the apical domain. The 6 A resolution cryo-EM GroEL structure clearly demonstrates the veracity and expanding scope of cryo-EM and the single particle reconstruction technique for macromolecular machines.
External linksStructure / PubMed:15242589
MethodsEM (single particle)
Resolution6.0 Å
Structure data

EMDB-1081:
Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy.
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • Escherichia coli (E. coli)

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