Crystals of family 11 xylanase II from Trichoderma longibrachiatum that diffract to atomic resolution

Acta Crystallographica Section D: Biological Crystallography

Volumn 60, Issue 7, 2004, Pages 1275-1277

  Moiseeva, Natalia ^a   Allaire, Marc ^a  

^a BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUNGI; TRICHODERMA; TRICHODERMA LONGIBRACHIATUM;

ENDO 1,4 BETA XYLANASE;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; PH; TRICHODERMA; X RAY CRYSTALLOGRAPHY;

CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ENDO-1,4-BETA XYLANASES; HYDROGEN-ION CONCENTRATION; TRICHODERMA;

EID: 16644389800     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444904009400     Document Type: Article

References (25)

1. Allaire, M., Aslantas, M., Berntson, A., Berman, L., Cheung, S., Clay, B., Greene, R., Jakoncic, J., Johnson, E., Kao, C.-C., Lenhard, A., Pjerov, S., Siddons, D. P., Stober, W., Venkatagiriyappa, V., Yin, Z. & Stojanoff, V. (2003). Synchrotron. Radiat. News, 16, 20-25.
2. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N. & Bourne, P. E. (2000). Nucleic Acids Res. 28, 235-242.
3. Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. F. Jr, Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977). J. Mol. Biol. 112, 535-542.
4. Campbell, R. L., Roes, D. R., Wakarchuk, R. J., To, R. J., Sung, W. & Yaguchi, M. (1993). Proceedings of the Second TRICEL Symposium on Trichoderma reesei Cellulases and Other Hydrolases, edited by P. Suominen & T. Reinikainen, pp. 63-72. Helsinki: Foundation for Biotechnical and Industrial Fermentation Research.
5. Chayen, N. (1999). Protein Crystallization, Techniques, Strategies and Tips, edited by T. Bergfors, pp. 219-248. La Jolla: International University Line.
6. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
7. Davies, G. & Henrissat, B. (1995). Structure, 3, 853-859.
8. French, G. S. & Wilson, K. S. (1978). Acta Cryst. A34, 517-525.
9. Fushinobu, S., Ito, K., Konno, M., Wakagi, T. & Matsuzawa, H. (1998). Protein Eng. 11, 1121-1128.
10. Gruber, K., Klintschar, G., Hayn, M., Schlacher, A., Steiner, W. & Kratky, C. (1998). Biochemistry, 37, 13475-13485.
11. Henrissat, B., Teeri, T. T. & Warren, R. A. J. (1998). FEBS Lett. 425, 352-354.
12. Jancarik, J. & Kim, S.-H. (1991). J. Appl. Cryst. 24, 409-111.
13. Krengel, U. & Dijkstra, B. W. (1996). J. Mol. Biol. 263, 70-78.
14. Kumar, S., Tsai, C.-J. & Nussinov, R. (2000). Protein Eng. 13, 179-191.
15. McCarthy, A. A., Morris, D. D., Bergquist, P. L. & Baker, E. N. (2000). Acta Cryst. D56, 1367-1375.
16. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-197.
17. Navaza, J. (1994). Acta Cryst. A50, 157-163.
18. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
19. Oakley, A., Heinrich, T., Thompson, C. & Wilce, M. (2003). Acta Cryst. D59, 627-636.
20. Sabini, E., Sulzenbacher, G., Dauter, M., Dauter, Z., Jorgensen, P. L., Schulein, M., Dupont, C., Davies, G. J. & Wilson, K. S. (1999). Chem. Biol. 6, 483-192.
21. Törrönen, A., Harkki, A. & Rouvinen, J. (1994). EMBO J. 13, 2493-2501.
22. Törrönen, A., Mach, R. L., Messner, R., Gonzales, R., Kalkkinen, N., Harkki, A. & Kubicek, C. P. (1992). Biotechnology, 10, 1461-1465.
23. Törrönen, A. & Rouvinen, J. (1995). Biochemistry, 34, 847-856.
24. Vagin, A. & Teplyakov, A. (1997). J. Appl. Cryst. 30, 1022-1025.
25. Wouters, J., Georis, J., Engher, D., Vandenhaute, J., Dusart, J., Frere, J. M., Depiereux, E. & Charlier, P. (2001). Acta Cryst. D57, 1813-1819.