Crystallization and preliminary X-ray crystallographic analysis of subunit F (F1-94), an essential coupling subunit of the eukaryotic V 1Vo-ATPase from Saccharomyces cerevisiae

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 9, 2012, Pages 1055-1059

  Basak, Sandip ^a   Balakrishna, Asha Manikkoth ^a   Manimekalai, Malathy Sony Subramanian ^a   Grüber, Gerhard ^a  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

Author keywords

Saccharomyces cerevisiae; selenomethionine; subunit F; V1VO ATPases

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SACCHAROMYCES CEREVISIAE PROTEIN; VMA7 PROTEIN, S CEREVISIAE;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; SACCHAROMYCES CEREVISIAE; X RAY CRYSTALLOGRAPHY;

CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; VACUOLAR PROTON-TRANSLOCATING ATPASES;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 84865733182     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112032526     Document Type: Article

References (21)

1. Basak, S., Gayen, S., Thaker, Y. R., Manimekalai, M. S. S., Roessle, M., Hunke, C. & Gruber, G. (2011). Biochim. Biophys. Acta, 1808, 360-368.
2. Beyenbach, K. W. & Wieczorek, H. (2006). J. Exp. Biol. 209, 577-589.
3. Coskun, U., Rizzo, V. F., Koch, M. H. J. & Gruber, G. (2004). J. Bioenerg. Biomembr. 36, 249-256.
4. Drory, O., Frolow, F. & Nelson, N. (2004). EMBO Rep. 5, 1148-1152.
5. Gruber, G., Godovac-Zimmermann, J., Link, T. A., Coskun, U., Rizzo, V. F., Betz, C. & Bailer, S. M. (2002). Biochem. Biophys. Res. Commun. 298, 383-391.
6. Gruber, G. & Marshansky, V. (2008). Bioessays, 30, 1096-1109.
7. Gruber, G., Radermacher, M., Ruiz, T., Godovac-Zimmermann, J., Canas, B., Kleine-Kohlbrecher, D., Huss, M., Harvey, W. R. & Wieczorek, H. (2000). Biochemistry, 39, 8609-8616.
8. Jancarik, J. & Kim, S.-H. (1991). J. Appl. Cryst. 24, 409-411.
9. Jefferies, K. C. & Forgac, M. (2007). J. Biol. Chem. 283, 4512-4519.
10. Laemmli, U. K. (1970). Nature (London), 227, 680-685.
11. Lolkema, J. S., Chaban, Y. & Boekema, E. J. (2003). J. Bioenerg. Biomembr. 35, 323-335.
12. Marshansky, V. (2007). Biochem. Soc. Trans. 35, 1092-1099.
13. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
14. Nishi, T. & Forgac, M. (2002). Nature Mol. Cell Biol. 30, 94-103.
15. Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
16. Parra, K. J., Keenan, K. L. & Kane, P. M. (2000). J. Biol. Chem. 275, 21761-21767.
17. Radermacher, M., Ruiz, T., Wieczorek, H. & Gruber, G. (2001). J. Struct. Biol. 135, 26-37.
18. Rishikesan, S., Gayen, S., Thaker, R. Y., Vivekanandan, S., Manimekalai, M. S. S., Yau, Y. H., Shochat, S. G. & Gruber, G. (2009). Biochim. Biophys. Acta, 1787, 242-251.
19. Rishikesan, S., Manimekalai, M. S. S. & Gruber, G. (2010). Biochim. Biophys. Acta, 1788, 1961-1968.
20. Sagermann, M., Stevens, T. H. & Matthews, B. W. (2001). Proc. Natl Acad. Sci. USA, 98, 7134-7139.
21. Saroussi, S. & Nelson, N. (2009). Eur. J. Physiol. 457, 581-587.