The three-dimensional structure of halorhodopsin to 5 Å by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 9, 2000, Pages 4637-4642

  Kunji, Edmund R S ^a   Von Gronau, Susanne ^b   Oesterhelt, Dieter ^b   Henderson, Richard ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BETA IONONE; HALORHODOPSIN; MEMBRANE PROTEIN; RETINAL;

ARTICLE; CALCULATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIFFRACTION; FOURIER TRANSFORMATION; HALOBACTERIUM SALINARUM; IMAGE ANALYSIS; IMAGE PROCESSING; PRIORITY JOURNAL;

BACTERIORHODOPSINS; CRYOELECTRON MICROSCOPY; FOURIER ANALYSIS; HALOBACTERIUM SALINARUM; HALORHODOPSINS; IMAGE PROCESSING, COMPUTER-ASSISTED; MODELS, MOLECULAR; PROTEIN CONFORMATION; SOFTWARE;

BACTERIA (MICROORGANISMS); HALOBACTERIUM SALINARUM;

EID: 0034712851     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.080064697     Document Type: Article

References (24)

1. Mukohata, Y., Ihara, K., Tamura, T. & Sugiyama, Y. (1999) J. Biochem. 125, 649-657.
2. Stoeckenius, W. (1999) Protein Sci. 8, 447-459.
3. Spudich, J. L. (1998) Mol. Microbiol. 28(6), 1051-1058.
4. Dér, A., Száraz, S., Tóth-Boconádi, R., Tokaji, Zs., Keszthelyi, L. & Stoeckenius, W. (1991) Proc. Natl. Acad. Sci. USA 88, 4751-4755.
5. Marti, T., Otto, H., Rösselet, S. J., Heyn, M. P. & Khorana, H. G. (1992) J. Biol. Chem. 267, 16922-16927.
6. Sasaki, J., Brown, L. S., Chon, Y.-S., Kandori, H., Maeda, A., Needleman, R. & Lanyi, J. K. (1995) Science 269, 73-75.
7. Tittor, J., Haupts, U., Haupts, C., Oesterhelt, D., Becker, A. & Bamberg, E. (1997) J. Mol. Biol. 271, 405-416.
8. Bamberg, E., Tittor, J. & Oesterhelt, D. (1993) Proc. Natl. Acad. Sci. USA 90, 639-643.
9. Váro, G., Brown, L. S., Needleman, R. & Lanyi, J. (1996) Biochemistry 35, 6604-6611.
10. Subramaniam, S. (1999) Curr. Opinion Struct. Biol. 9, 462-468.
11. Havelka, W. A., Henderson, R., Heymann, J. A. W. & Oesterhelt, D. (1993) J. Mol. Biol. 234, 837-846.
12. Havelka, W. A., Henderson, R. & Oesterhelt, D. (1995) J. Mol. Biol. 247, 726-738.
13. Heymann, J. A., Havelka W. A. & Oesterhelt, D. (1993) Mol. Microbiol. 7(4), 623-630.
14. Bullough, P. A. & Henderson, R. (1987) Ultramicroscopy 21, 223-230.
15. Crowther, R. A., Henderson, R. & Smith, J. M. (1996) J. Struct. Biol. 116, 9-16.
16. Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. & Downing, K. H. (1990) J. Mol. Biol. 213, 899-929.
17. Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M. & Henderson, R. (1996) J. Mol. Biol. 259(3), 393-421.
18. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991) Acta Crystallogr. A 47, 110-119.
19. Kühlbrandt, W., Wang, D. N. & Fujijoshi, Y. (1994) Nature (London) 367, 614-621.
20. Henderson, R. (1995) Q. Rev. Biophys. 28, 171-193.
21. Wang, D. N. & Kühlbrandt, W. (1991) J. Mol. Biol. 217, 691-699.
22. Waltz, T., Hirai, T., Murata, K., Heymann, J. B., Mitsuoka, K., Fujiyoshi, Y., Smith, B. L., Agre, P. & Engel, A. (1997) Nature (London) 387, 624-627.
23. Nogales, E., Wolf, S. G. & Downing, K. H. (1998) Nature (London) 391, 199-203.
24. Grigorieff, N., Beckmann, E. & Zemlin, F. (1995) J. Mol. Biol. 254(30), 404-415.