Crystallization and preliminary X-ray analysis of Acetivibrio cellulolyticus cellulosomal type II cohesin module: Two versions having different linker lengths

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 64, Issue 1, 2008, Pages 58-61

  Noach, Ilit ^a   Alber, Orly ^a   Bayer, Edward A ^a   Lamed, Raphael ^b   Levy Assaraf, Maly ^b   Shimon, Linda J W ^a   Frolow, Felix ^b  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

Cellulosome; Cohesin type II; Linkers

Indexed keywords

ACETIVIBRIO CELLULOLYTICUS;

EID: 37549050605     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309107066821     Document Type: Article

References (25)

1. Adams, J. J., Pal, G., Jia, Z. & Smith, S. P. (2006). Proc. Natl Acad. Sci. USA, 103, 305-310.
2. Bayer, E. A., Belaich, J.-P., Shoham, Y. & Lamed, R. (2004). Annu. Rev. Microbiol. 58, 521-554.
3. Bayer, E. A., Morag, E. & Lamed, R. (1994). Trends Biotechnol. 12, 378-386.
4. Bayer, E. A., Shoham, Y. & Lamed, R. (2000). The Prokaryotes: An Evolving Electronic Resource for the Microbiological Community, 3rd ed., edited by E. Stackebrandt. New York: Springer-Verlag.
5. Carvalho, A. L., Dias, F. M., Prates, J. A., Nagy, T., Gilbert, H. J., Davies, G. J., Ferreira, L. M., Romão, M. J. & Fontes, C. M. (2003). Proc. Natl Acad. Sci. USA, 100, 13809-13814.
6. Carvalho, A. L., Pires, V. M., Gloster, T. M., Turkenburg, J. P., Prates, J. A., Ferreira, L. M., Romao, M. J., Davies, G. J., Fontes, C. M. & Gilbert, H. J. (2005). J. Mol. Biol. 349, 909-915.
7. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
8. Cosier, J. & Glazer, A. M. (1986). J. Appl. Cryst. 19, 105-107.
9. Ding, S.-Y., Bayer, E. A., Steiner, D., Shoham, Y. & Lamed, R. (1999). J. Bacteriol. 181, 6720-6729.
10. Lamed, R., Setter, E. & Bayer, E. A. (1983). J. Bacteriol. 156, 828-836.
11. Lamed, R., Setter, E., Kenig, R. & Bayer, E. A. (1983). Biotechnol. Bioeng. Symp. 13, 163-181.
12. Leibovitz, E. & Béguin, P. (1996). J. Bacteriol. 178, 3077-3084.
13. Lytle, B., Myers, C., Kruus, K. & Wu, J. H. D. (1996). J. Bacteriol. 178, 1200-1203.
14. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
15. Noach, I., Frolow, F., Jakoby, H., Rosenheck, S., Shimon, L. J. W., Lamed, R. & Bayer, E. A. (2005). J. Mol. Biol. 348, 1-12.
16. Noach, I., Lamed, R., Xu, Q., Rosenheck, S., Shimon, L. J. W., Bayer, E. A. & Frolow, F. (2003). Acta Cryst. D59, 1670-1673.
17. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
18. Salamitou, S., Raynaud, O., Lemaire, M., Coughlan, M., Béguin, P. & Aubert, J.-P. (1994). J. Bacteriol. 176, 2822-2827.
19. Shimon, L. J. W., Frolow, F., Yaron, S., Bayer, E. A., Lamed, R., Morag, E. & Shohan, Y. (1997). Acta Cryst. D53, 114-115.
20. Stout, G. H. & Jensen, L. H. (1968). X-ray Structure Determination. A Practical Guide, p. 402. London: Macmillan.
21. Spinelli, S., Fierobe, H. P., Belaich, A., Belaich, J. P., Henrissat, B. & Cambillau, C. (2000). J. Mol. Biol. 304, 189-200.
22. Tavares, G. A., Béguin, P. & Alzari, P. M. (1997). J. Mol. Biol. 273, 701-713.
23. Vagin, A. & Teplyakov, A. (1997). J. Appl. Cryst. 30, 1022-1025.
24. Woessner, J. P. & Goodenough, U. W. (1992). Plant Sci. 83, 65-76.
25. Xu, Q., Gao, W., Ding, S.-Y., Kenig, R., Shoham, Y., Bayer, E. A. & Lamed, R. (2003). J. Bacteriol. 185, 4548-4557.