A 11.5 Å single particle reconstruction of GroEL using EMAN

Journal of Molecular Biology

Volumn 314, Issue 2, 2001, Pages 253-262

  Ludtke, Steven J ^a   Jakana, Joanita ^a   Song, Jiu Li ^b   Chuang, David T ^b   Chiu, Wah ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Electron cryomicroscopy; GroEL; Single particle reconstruction; Structure; X ray scattering

Indexed keywords

CHAPERONIN; ESCHERICHIA COLI PROTEIN;

ANIMAL CELL; ARTICLE; BACTERIAL MEMBRANE; CONTROLLED STUDY; CRYSTAL STRUCTURE; IMAGE RECONSTRUCTION; IN VITRO STUDY; INTERMETHOD COMPARISON; MACROMOLECULE; NONHUMAN; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; VALIDATION PROCESS; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER PROGRAM; COMPUTER SIMULATION; CRYOELECTRON MICROSCOPY; PROTEIN CONFORMATION; REPRODUCIBILITY; X RAY DIFFRACTION;

BACTERIA (MICROORGANISMS);

COMPUTER SIMULATION; CRYOELECTRON MICROSCOPY; ESCHERICHIA COLI PROTEINS; GROEL PROTEIN; MODELS, MOLECULAR; PROTEIN CONFORMATION; REPRODUCIBILITY OF RESULTS; SOFTWARE; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; X-RAY DIFFRACTION;

EID: 0035940689     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5133     Document Type: Article

References (20)

1. Molecular machines: Putting the pieces together
2. Fourier amplitude decay of electron cryo-microscopic images of single particles and effects on structure determination
3. EMAN: Semiautomated software for high-resolution single-particle reconstructions
4. Structure and function in GroEL-mediated protein folding
5. GroEL/GroES: Structure and function of a two-stroke folding machine
6. Chaperone-assisted protein folding
7. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
8. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
9. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
10. Electron microscopy study of GroEL chaperonin: Different views of the aggregate appear as a function of cell growth temperature
11. Structural basis of allosteric changes in the GroEL mutant Arg197 → Ala
12. Solution structure of the E. coli 70S ribosome at 11.5 Å resolution
13. A dynamic model for the allosteric mechanism of GroEL
14. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
15. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
16. GroEL/GroES-dependent reconstitution of alpha2 beta2 tetramers of humanmitochondrial branched chain alpha-ketoacid decarboxylase. Obligatory interaction of chaperonins with an alpha beta dimeric intermediate
17. The origins and consequences of asymmetry in the chaperonin reaction cycle
18. A wide bandpass multilayer monochromator for biological small angle scattering and diffraction
19. The Fourier transform of an electron micrograph: Effects of defocusing and aberrations, and implications for the use of underfocus contrast enhancement