Cloning, expression, crystallization and preliminary X-ray studies of the ferredoxin-NAD(P)+ reductase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 9, 2012, Pages 1048-1051

  Liauw, Pasqual ^a   Mashiba, Tomohiro ^b   Kopczak, Marta ^a   Wiegand, Katrin ^a   Muraki, Norifumi ^c   Kubota, Hisako ^c   Kawano, Yusuke ^b   Ikeuchi, Masahiko ^b   Hase, Toshiharu ^c   Rögner, Matthias ^a   Kurisu, Genji ^c  

^a RUHR UNIVERSITY BOCHUM   (Germany)

^b UNIVERSITY OF TOKYO   (Japan)

^c OSAKA UNIVERSITY   (Japan)

Author keywords

electron transfer complexes; ferredoxin; ferredoxin NADP+ reductase

Indexed keywords

FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; CYANOBACTERIUM; ENZYMOLOGY; GENE EXPRESSION; GENETICS; MOLECULAR CLONING; X RAY CRYSTALLOGRAPHY;

CLONING, MOLECULAR; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYANOBACTERIA; FERREDOXIN-NADP REDUCTASE; GENE EXPRESSION;

CYANOBACTERIA; THERMOSYNECHOCOCCUS ELONGATUS BP-1;

EID: 84865742656     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112031910     Document Type: Article

References (18)

1. Aliverti, A., Pandini, V., Pennati, A., de Rosa, M. & Zanetti, G. (2008). Arch. Biochem. Biophys. 474, 283-291.
2. Avron, M. & Jagendorf, A. T. (1956). Arch. Biochem. Biophys. 65, 475-490.
3. Gómez-Lojero, C., Pérez-Gómez, B., Shen, G., Schluchter, W. M. & Bryant, D. A. (2003). Biochemistry, 42, 13800-13811.
4. Hanke, G. T., Kurisu, G., Kusunoki, M. & Hase, T. (2004). Photosynth. Res. 81, 317-327.
5. Hurley, J. K., Morales, R., Martínez-Júlvez, M., Brodie, T. B., Medina, M., Gómez-Moreno, C. & Tollin, G. (2002). Biochim. Biophys. Acta, 1554, 5-21.
6. Karplus, P. A., Daniels, M. J. & Herriott, J. R. (1991). Science, 251, 60-66.
7. Long, F., Vagin, A. A., Young, P. & Murshudov, G. N. (2008). Acta Cryst. D64, 125-132.
8. Lorimier, R. de, Guglielmi, G., Bryant, D. A. & Stevens, S. E. (1990). Arch. Microbiol. 153, 541-549.
9. Nakajima, M., Sakamoto, T. & Wada, K. (2002). Plant Cell Physiol. 43, 484-493.
10. Nakamura, Y. et al. (2002). DNA Res. 9, 123-130.
11. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
12. Rowell, P., Diez, J., Apte, S. K. & Stewart, W. D. (1981). Biochim. Biophys. Acta, 657, 507-516.
13. Schluchter, W. M. & Bryant, D. A. (1991). Biochemistry, 31, 3092-3102.
14. Schulz, G. E., Schirmer, R. H., Sachsenheimer, W. & Pai, E. F. (1978). Nature (London), 273, 120-124.
15. Serre, L., Vellieux, F. M., Medina, M., Gomez-Moreno, C., Fontecilla-Camps, J. C. & Frey, M. (1996). J. Mol. Biol. 263, 20-39.
16. Thor, J. J. van, Gruters, O. W., Matthijs, H. C. & Hellingwerf, K. J. (1999). EMBO J. 18, 4128-4136.
17. Thor, J. J. van, Hellingwerf, K. J. & Matthijs, H. C. (1998). Plant Mol. Biol. 36, 353-363.
18. Yamaoka, T., Satoh, K. & Satoh, S. (1978). Plant Cell Physiol. 19, 943-954.