Overexpression, purification, crystallization and preliminary X-ray analysis of Rv2780 from Mycobacterium tuberculosis H37Rv

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 64, Issue 5, 2008, Pages 367-370

  Tripathi, Sarvind Mani ^a   Ramachandran, Ravishankar ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

Alanine dehydrogenase; Antigen; Latent stage; Mycobacterium tuberculosis; NAD; Rv2780

Indexed keywords

ALANINE DEHYDROGENASE; BACTERIAL PROTEIN; GLYCOSYLTRANSFERASE; RECOMBINANT PROTEIN; RV2957 PROTEIN, MYCOBACTERIUM TUBERCULOSIS;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MYCOBACTERIUM TUBERCULOSIS; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ALANINE DEHYDROGENASE; BACTERIAL PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLTRANSFERASES; MYCOBACTERIUM TUBERCULOSIS; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

CORYNEBACTERINEAE; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 43049134487     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309108007653     Document Type: Article

References (28)

1. Agren, D., Stehr, M., Berthold, C. L., Kapoor, S., Oehlmann, W., Singh, M. & Schneider, G. (2008). J. Mol. Biol. 377, 1161-1173.
2. Andersen, A. B., Andersen, P. & Ljungqvist, L. (1992). Infect. Immun. 60, 2317-2323.
3. Baker, P. J., Sawa, Y., Shibata, H., Sedelnikova, S. E. & Rice, D. W. (1998). Nature Struct. Biol. 5, 561-567.
4. Baker, P. J., Turnbull, A. P., Sedelnikova, S. E., Stillman, T. J. & Rice, D. W. (1995). Structure, 3, 693-705.
5. Betts, J. C., Lukey, P. T., Robb, L. C., McAdam, R. A. & Duncan, K. (2002). Mol. Microbiol. 43, 717-731.
6. Bradford, M. M. (1976). Anal. Biochem. 72, 248-254.
7. Chan, K., Knaak, T., Satkamp, L., Humbert, O., Falkow, S. & Ramakrishnan, L. (2002). Proc. Natl Acad. Sci. USA, 99, 3920-3925.
8. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
9. Cudney, R., Patel, S., Weisgraber, K., Newhouse, Y. & McPherson, A. (1994). Acta Cryst. D50, 414-423.
10. Gallagher, D. T., Monbouquette, H. G., Schroder, I., Robinson, H., Holden, M. J. & Smith, N. N. (2004). J. Mol. Biol. 342, 119-130.
11. Hasan, S., Daugelat, S., Srinivasa Rao, P. S. & Schreiber, M. (2006). PLOS Comput. Biol. 2, e61.
12. Itoh, N. & Morikawa, R. (1983). Agric. Biol. Chem. 47, 2511-2519.
13. Jancarik, J. & Kim, S.-H. (1991). J. Appl. Cryst. 24, 409-411.
14. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
15. Mazeed, S., Ofek, G., Belachew, A., Huang, C. C., Zhou, T. & Kwong, P. D. (2003). Structure, 11, 1061-1070.
16. Navaza, J. (1994). Acta Cryst. A50, 157-163.
17. Ohshima, T., Sakane, M., Yamazaki, T. & Soda, K. (1990). Eur. J. Biochem. 191, 715-720.
18. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
19. Rosenkrands, I., Slayden, R. A., Crawford, J., Aagaard, C., Barry, C. E. III & Andersen, P. (2002). J. Bacteriol. 184, 3485-3491.
20. Sawa, Y., Tani, M., Murata, K., Shibata, H. & Ochiai, H. (1994). J. Biochem. 116, 995-1000.
21. Siranosian, K. J., Ireton, K. & Grossman, A. D. (1993). J. Bacteriol. 175, 6789-6796.
22. Stewart, G. R., Robertson, B. D. & Young, D. B. (2003). Nature Rev. Microbiol. 2, 97-105.
23. Stillman, T. J., Baker, P. J., Britton, K. L. & Rice, D. W. (1993). J. Mol. Biol. 234, 1131-1139.
24. Usha, V., Jayaraman, R., Toro, J. C., Hoffner, S. E. & Das, K. S. (2002). Can. J. Microbiol. 48, 7-13.
25. Vanhooke, J. L., Thoden, J. B., Brunhuber, N. M. W., Blanchard, J. S. & Holden, H. M. (1999). Biochemistry, 38, 2326-2339.
26. Vancura, A., Vancurová, I., Volc, J., Jones, S. K., Flieger, M., Basarová, G. & Behal, V. (1989). Eur. J. Biochem. 15, 221-227.
27. Vancurova, I., Vancura, A., Volc, J., Neuzil, J. & Behal, V. (1989). J. Basic Microbiol. 29, 185-189.
28. Ward, M. J., Lew, H. & Zusman, D. R. (2000). J. Bacteriol. 182, 546-550.