Purification, crystallization and preliminary X-ray diffraction analysis of Methanococcus jannaschii TATA box-binding protein (TBP)

Acta Crystallographica Section D: Biological Crystallography

Volumn 60, Issue 12 II, 2004, Pages 2328-2331

  Adachi, Naruhiko ^a,b   Natsume, Ryo ^c   Senda, Miki ^c   Muto, Shinsuke ^a,b   Senda, Toshiya ^d   Horikoshi, Masami ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c Japan Biological Information Research Center   (Japan)

^d NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

METHANOCALDOCOCCUS JANNASCHII; SULFOLOBUS ACIDOCALDARIUS;

TATA BINDING PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; DIFFUSION; ESCHERICHIA COLI; HUMAN; METABOLISM; METHANOCOCCUS; MOLECULAR GENETICS; PHYLOGENY; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; SEQUENCE HOMOLOGY; SULFOLOBUS ACIDOCALDARIUS; TEMPERATURE; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIFFUSION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HUMANS; METHANOCOCCUS; MOLECULAR SEQUENCE DATA; PHYLOGENY; PLASMIDS; SEQUENCE HOMOLOGY, AMINO ACID; SULFOLOBUS ACIDOCALDARIUS; TATA-BOX BINDING PROTEIN; TEMPERATURE; X-RAY DIFFRACTION;

EID: 21644484800     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444904023960     Document Type: Article

References (33)

1. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, G. L. (1998). Acta Cryst. D54, 905-921.
2. Chasman, D. I., Flaherty, K. M., Sharp, P. A. & Kornberg, R. D. (1993). Proc. Natl Acad. Sci. USA, 90, 8174-8178.
3. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
4. DeDecker, B. S., O'Brien, R., Fleming, P. J., Geiger, J. H., Jackson, S. P. & Sigler, P. B. (1996). J. Mol. Biol. 264, 1072-1084.
5. Gasch, A., Hoffmann, A., Horikoshi, M., Roeder, R. G. & Chua, N. H. (1990). Nature (London), 346, 390-394.
6. Hoffmann, A., Horikoshi, M., Wang, C. K., Schroeder, S., Weil, P. A. & Roeder, R. G. (1990). Genes Dev. 4, 1141-1148.
7. Hoffmann, A., Sinn, E., Yamamoto, T., Wang, J., Roy, A., Horikoshi, M. & Roeder, R. G. (1990). Nature (London), 346, 387-390.
8. Horikoshi, M., Bēṙtuccioli, C., Takada, R., Wang, J., Yamamoto, T. & Roeder, R. G. (1992). Proc. Natl Acad. Sci. USA, 89, 1060-1064.
9. Horikoshi, M., Wang, C. K., Fujii, H., Cromlish, J. A., Weil, P. A. & Roeder, R. G. (1989a). Proc. Natl Acad. Sci. USA, 86, 4843-4847.
10. Horikoshi, M., Wang, C. K., Fujii, H., Cromlish, J. A., Weil, P. A. & Roeder, R. G. (1989b). Nature (London), 341, 299-303.
11. Horikoshi, M., Yamamoto, T., Ohkuma, Y., Weil, P. A. & Roeder, R. G. (1990). Cell, 61, 1171-1178.
12. Juo, Z. S., Chiu, T. K., Leiberman, P. M., Baikalov, I., Berk, A. J. & Dickerson, R. E. (1996). J. Mol. Biol. 261, 239-254.
13. Kim, J. L., Nikolov, D. B. & Burley, S. K. (1993). Nature (London), 400, 520-527.
14. Kim, T. K., Hashimoto, S., Kelleher, R. J. III, Flanagan, P. M., Kornberg, R. D., Horikoshi, M. & Roeder, R. G. (1994). Nature (London), 369, 252-255.
15. Koike, H., Kawashima-Ohya, Y., Yamasaki, T., Clowney, L., Katsuya, Y. & Suzuki, M. (2004). Structure, 12, 157-168.
16. Kosa, P. F., Ghosh, G., DeDecker, B. S. & Sigler, P. B. (1997). Proc. Natl Acad. Sci. USA, 94, 6042-6047.
17. Lee, D. K., Horikoshi, M. & Roeder, R. G. (1991). Cell, 67, 1241-1250.
18. Littlefield, O., Korkhin, Y. & Sigler, P. B. (1999). Proc. Natl Acad. Sci. USA, 96, 13668-13673.
19. Marsh, T. L., Reich, C. I., Whitelock, R. B. & Olsen, G. J. (1994). Proc. Natl Acad. Sci. USA, 91, 4180-4184.
20. Munich, M. L., Iida, C. T., Horikoshi, M., Roeder, R. G. & Parker, C. S. (1990). Proc. Natl Acad. Sci. USA, 87, 9148-9152.
21. Nikolov, D. B., Chen, H., Halay, E. D., Hoffmann, A., Roeder, R. G. & Burley, S. K. (1996). Proc. Natl Acad. Sci. USA, 93, 4862-4867.
22. Nikolov, D. B., Hu, S. H., Lin, J., Gasch, A., Hoffmann, A., Horikoshi, M., Chua, N. H., Roeder, R. G. & Burley, S. K. (1992). Nature (London), 360, 40-46.
23. Ouhammouch, M., Dewhurst, R. E., Hausner, W., Thomm, M. & Geiduschek, E. P. (2003). Proc. Natl Acad. Sci. USA, 100, 5097-5102.
24. Patikoglou, G. A., Kim, J. L., Sun, L., Yang, S. H., Kodadek, T. & Burley, S. K. (1999). Genes Dev. 13, 3217-3230.
25. Poon, D., Knittle, R. A., Sabelko, K. A., Yamamoto, T., Horikoshi, M., Roeder, R. G. & Weil, P. A. (1993). J. Biol. Chem. 268, 5005-5013.
26. Reeve, J. N. (2003). Mol. Microbiol. 48, 587-598.
27. Roeder, R. G. (1996). Trends Biochem. Sci. 21, 327-335.
28. Rowlands, T., Baumann, P. & Jackson, S. P. (1994). Science, 264, 1326-1329.
29. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). Nucleic Acids Res. 22, 4673-4680.
30. Vagin, A. & Teplyakov, A. (1997). J. Appl. Cryst. 30, 1022-1025.
31. Wettach, J., Gohl, H. P., Tschochner, H. & Thomm, M. (1995). Proc. Natl Acad. Sci. USA, 92, 472-476.
32. Woychik, N. A. & Hampsey, M. (2002). Cell, 108, 453-463.
33. Yamamoto, T., Horikoshi, M., Wang, J., Hasegawa, S., Weil, P. A. & Roeder, R. G. (1992). Proc. Natl Acad. Sci. USA, 89, 2844-2848.