Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 11, 2012, Pages 1387-1389

  Safonova, Tatyana N ^a   Mordkovich, Nadezhda N ^a   Polyakov, Konstantin M ^a,b   Manuvera, Valentin A ^c   Veiko, Vladimir P ^a   Popov, Vladimir O ^a  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

^b ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^c FEDERAL RESEARCH AND CLINICAL CENTER OF PHYSICAL CHEMICAL MEDICINE OF FEDERAL MEDICAL BIOLOGICAL AGENCY   (Russian Federation)

Author keywords

crystallization under microgravity; Shewanella oneidensis MR 1; uridine; uridine phosphorylase

Indexed keywords

BACTERIAL PROTEIN; URIDINE; URIDINE PHOSPHORYLASE;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; SHEWANELLA; WEIGHTLESSNESS; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; SHEWANELLA; URIDINE; URIDINE PHOSPHORYLASE; WEIGHTLESSNESS;

ESCHERICHIA COLI; SHEWANELLA ONEIDENSIS MR-1;

EID: 84869012776     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112041784     Document Type: Article

References (18)

1. Cao, D., Ziemba, A., McCabe, J., Yan, R.,Wan, L., Kim, B., Gach, M., Flynn, S. & Pizzorno, G. (2011). Mol. Cancer Ther. 10, 2330-2339.
2. Caradoc-Davies, T. T., Cutfield, S. M., Lamont, I. L. & Cutfield, J. F. (2004). J. Mol. Biol. 337, 337-354.
3. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
4. Kanzaki, A., Takebayashi, Y., Bando, H., Eliason, J. F., Watanabe Si, S., Miyashita, H., Fukumoto, M., Toi, M. & Uchida, T. (2002). Int. J. Cancer, 97, 631-635.
5. Krenitsky, T. A., Mellors, J. W. & Barclay, R. K. (1965). J. Biol. Chem. 240, 1281-1286.
6. Laemmli, U. K. (1970). Nature (London), 227, 680-685.
7. Lanthier, M., Gregory, K. B. & Lovley, D. R. (2008). FEMS Microbiol. Lett. 278, 29-35.
8. Lovley, D. R. (2008). Curr. Opinion Biotechnol. 19, 1-8.
9. Mordkovich, N. N., Manuvera, V. A., Veiko, V. P. & Debabov, V. G. (2012). Biotekhnologiia (Moscow), 1, 21-30.
10. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
11. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
12. Paul, D., O'Leary, S. E., Rajashankar, K., Bu, W., Toms, A., Settembre, E. C., Sanders, J. M., Begley, T. P. & Ealick, S. E. (2010). Biochemistry, 49, 3499- 3509.
13. Pugmire, M. J. & Ealick, S. E. (2002). Biochem. J. 361, 1-25.
14. Roosild, T. P., Castronovo, S., Fabbiani, M. & Pizzorno, G. (2009). BMC Struct. Biol. 9, 14.
15. Takahashi, S., Tsurumura, T., Aritake, K., Furubayashi, N., Sato, M., Yamanaka, M., Hirota, E., Sano, S., Kobayashi, T., Tanaka, T., Inaka, K., Tanaka, H. & Urade, Y. (2010). Acta Cryst. F66, 846-850.
16. Tran, T. H., Christoffersen, S., Allan, P. W., Parker, W. B., Piskur, J., Serra, I., Terreni, M. & Ealick, S. E. (2011). Biochemistry, 50, 6549-6558.
17. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
18. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.