Crystallization and preliminary X-ray diffraction studies of the precursor protein of a thermostable variant of papain

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 67, Issue 5, 2011, Pages 634-636

  Roy, Sumana ^a   Choudhury, Debi ^a   Chakrabarti, Chandana ^a   Biswas, Sampa ^a   Dattagupta, J K ^a  

^a SAHA INSTITUTE OF NUCLEAR PHYSICS   (India)

Author keywords

cysteine proteases; pro papain; thermostable variants

Indexed keywords

PAPAIN; PROTEIN PRECURSOR;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYME STABILITY; MOLECULAR GENETICS; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; PAPAIN; PROTEIN PRECURSORS; TEMPERATURE;

ESCHERICHIA COLI;

EID: 79955664130     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309111010888     Document Type: Article

References (19)

1. Baker, D., Silen, J. L. & Agard, D. A. (1992). Proteins, 12, 339-344.
2. Brocklehurst, K., Salih, E., McKee, R. & Smith, H. (1985). Biochem. J. 228, 525-527.
3. Choudhury, D., Biswas, S., Roy, S. & Dattagupta, J. K. (2010). Protein Eng. Des. Sel. 23, 457-467.
4. Choudhury, D., Roy, S., Chakrabarti, C., Biswas, S. & Dattagupta, J. K. (2009). Phytochemistry, 70, 465-472.
5. Dickinson, D. P. (2002). Crit. Rev. Oral Biol. Med. 13, 238-275.
6. Drenth, J., Jansonius, J. N., Koekoek, R., Swen, H. M. &Wolthers, B. G. (1968). Nature (London), 218, 929-932.
7. Fox, T., de Miguel, E., Mort, J. S. & Storer, A. C. (1992). Biochemistry, 31, 12571-12576.
8. Fukuda, R., Horiuchi, H., Ohta, A. & Tagagi, M. (1994). J. Biol. Chem. 269, 9551-9561.
9. Groves, M. R., Taylor, M. A., Scott, M., Cummings, N. J., Pickersgill, R. W. & Jenkins, J. A. (1996). Structure, 4, 1193-1203.
10. Grzonka, Z., Kasprzykowski, F. & Wiczk, W. (2007). Industrial Enzymes: Structure, Function and Applications, edited by J. Polaina & A. P. MacCabe, pp. 181-195. Dordrecht: Springer.
11. Kamphuis, I. G., Kalk, K. H., Swarte, M. B. & Drenth, J. (1984). J. Mol. Biol. 179, 233-256.
12. Mach, L., Mort, J. S. & Glössl, J. (1994). J. Biol. Chem. 269, 13030-13035.
13. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
14. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
15. Taylor, M. A., Baker, K. C., Briggs, G. S., Connerton, I. F., Cummings, N. J., Pratt, K. A., Revell, D. F., Freedman, R. B. & Goodenough, P. W. (1995). Protein Eng. 8, 59-62.
16. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
17. Wetmore, D. R., Wong, S.-L. & Roche, R. S. (1992). Mol. Microbiol. 6, 1593-1604.
18. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
19. Winther, J. R. & Sørensen, P. (1991). Proc. Natl Acad. Sci. USA, 88, 9330-9334.