Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules

Journal of Structural Biology

Volumn 116, Issue 1, 1996, Pages 155-160

  Yasunaga, Takuo ^a   Wakabayashi, Takeyuki ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CHEMICAL STRUCTURE; COMPUTER PROGRAM; ELECTRON MICROSCOPY; IMAGE ANALYSIS; MACROMOLECULE; PRIORITY JOURNAL;

EOS;

EID: 0029881549     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1996.0025     Document Type: Article

References (20)

1. Amos, L. A., and Klug, A. (1975) Three-dimensional image reconstruction of the contractile tail of T4 bacteriophage, J. Mol. Biol. 99, 51-73.
2. Brünger, A. T. (1992) X-PLOR, Yale Univ. Press, New Haven/ London.
3. DeRosier, D. J., and Moore, P. B. (1970) Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry, J. Mol. Biol. 52, 355-369.
4. Frank, J., Shimkin, B., and Dowse, H. (1981) Spider - A modular software system for electron image processing, Ultramicroscopy, 6, 343-358.
5. Frank, J., and Radermacher, M. (1992) Three-dimensional reconstruction of single particles negatively stained or in vitreous ice, Ultramicroscopy, 46, 241-262.
6. Fujiyama, Y., Yokoyama, K., Yoshida, M., and Wakabayashi, T. (1990) Electron microscopy of the reconstituted complexes of the F1-ATPase with various subunit constitution revealed the location of the gamma-subunit in the central cavity of the molecule, FEBS Lett. 271, 111-115.
7. Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, C. F., Beckmann, E., and Downing, K. H. (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy, J. Mol. Biol. 213, 899-929.
8. Jones, T. A. (1978) A graphics model building and refinement system for macromolecules, J. Appl. Crystallogr. 11, 268-272.
9. Jones, T. A. (1982) TOM: A graphics fitting program for macromolecules, in Sayre, D. (Ed.), Computational Crystallography, pp. 303-317, Clarendon Press, Oxford.
10. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
11. Klug, A., Crick, F. H. C., and Wyckoff, H. W. (1958) Diffraction by helical structures, Acta Crystallogr. 11, 199-213.
12. Konstantinides, K., and Rasure, J. (1994) The khoros software development environment for image and signal processing, IEEE Trans. Image Processing 3, 243-252.
13. Lorenz, M., Popp, D., and Holmes, K. C. (1993) Refinement of the F-actin model against X-ray fibre diffraction data by the use of a directed mutation algorithm, J. Mol. Biol. 234, 826-836.
14. Moore, P. B., Huxley, H. E., and DeRosier, D. J. (1970) Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments, J. Mol. Biol. 50, 279-295.
15. Saxton, W. O., Pitt, T. J., and Horner, M. (1979) Digital image processing: The Semper system, Ultramicroscopy 4, 343-354.
16. 2-macroglobulin: Concordance between projected views obtained by negative-stain and cryo-electron microscopy, J. Struct. Biol. 106, 172-178.
17. Toyoshima, C., and Wakabayashi, T. (1985) Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin-myosin subfragment-1 complex, J. Biochem. 97, 245-263.
18. van Heel, M., and Frank, J. (1981) Use of multivariate statistics in analyzing the images of biological macromolecules, Ultramicroscopy 6, 187-194.
19. van Heel, M., and Keegstra, W. (1981) IMAGIC: A fast, flexible and friendly image analysis software system, Ultramicroscopy 7, 113-130.
20. Wakabayashi, T., Huxley, H. E., Amos, L. A., and Klug, A. (1975) Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complex, J. Mol. Biol. 93, 477-497.