Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana

. 2009 May 01 ; 65 (Pt 5) : 478-81. [epub] 20090424

Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid19407381

The receiver domain (RD) of a sensor histidine kinase (HK) catalyses the transphosphorylation reaction during the action of HKs in hormonal and abiotic signalling in plants. Crystals of the recombinant RD of the Arabidopsis thaliana HK CYTOKININ-INDEPENDENT1 (CKI1(RD)) have been obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant and glycerol as a cryoprotectant. The crystals diffracted to approximately 2.4 A resolution on beamline BW7B of the DORIS-III storage ring. The diffraction improved significantly after the use of a non-aqueous cryoprotectant. Crystals soaked in Paratone-N diffracted to at least 2.0 A resolution on beamline BW7B and their mosaicity decreased more than tenfold. The crystals belonged to space group C222(1), with unit-cell parameters a = 54.46, b = 99.82, c = 79.94 A. Assuming the presence of one molecule of the protein in the asymmetric unit gives a Matthews coefficient V(M) of 2.33 A(3) Da(-1). A molecular-replacement solution has been obtained and structure refinement is in progress.

Zobrazit více v PubMed

Bradford, M. M. (1976). Anal. Biochem.72, 248–254. PubMed

Calva, E. & Oropeza, R. (2006). Microb. Ecol.51, 166–176. PubMed

Chang, C. & Stewart, R. C. (1998). Plant Physiol.117, 723–731. PubMed PMC

Cohen, S. X., Ben Jelloul, M., Long, F., Vagin, A., Knipscheer, P., Lebbink, J., Sixma, T. K., Lamzin, V. S., Murshudov, G. N. & Perrakis, A. (2008). Acta Cryst. D64, 49–60. PubMed PMC

Hwang, I. & Sheen, J. (2001). Nature (London), 413, 383–389. PubMed

Hoch, J. A. (2000). Curr. Opin. Microbiol.3, 165–170. PubMed

Kabsch, W. (1993). J. Appl. Cryst.26, 795–800.

Kakimoto, T. (1996). Science, 274, 982–985. PubMed

Keegan, R. M. & Winn, M. D. (2007). Acta Cryst. D63, 447–457. PubMed

Laemmli, U. K. (1970). Nature (London), 227, 680–685. PubMed

Matthews, B. W. (1968). J. Mol. Biol.33, 491–497. PubMed

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst.40, 658–674. PubMed PMC

Mizuno, T. (2005). Biosci. Biotechnol. Biochem.69, 2263–2276. PubMed

Muller-Dieckmann, H. J., Grantz, A. A. & Kim, S.-H. (1999). Structure, 7, 1547–1556. PubMed

Murshudov, G. N., Vagin, A. A. & Dodson, E. J. (1997). Acta Cryst. D53, 240–255. PubMed

Notredame, C., Higgins, D. & Heringa, J. (2000). J. Mol. Biol.302, 205–217. PubMed

Skerker, J. M., Perchuk, B. S., Siryaporn, A., Lubin, E. A., Ashenberg, O., Goulian, M. & Laub, M. T. (2008). Cell, 133, 1043–1054. PubMed PMC

Sola, M., Gomis-Ruth, F. X., Serrano, L., Gonzalez, A. & Coll, M. (1999). J. Mol. Biol.285, 675–687. PubMed

Stock, A. M., Mottonen, J. M., Stock, J. B. & Schutt, C. E. (1989). Nature (London), 337, 745–749. PubMed

To, J. P. & Kieber, J. J. (2008). Trends Plant Sci.13, 85–92. PubMed

Tran, L. S., Urao, T., Qin, F., Maruyama, K., Kakimoto, T., Shinozaki, K. & Yamaguchi-Shinozaki, K. (2007). Proc. Natl Acad. Sci. USA, 104, 20623–20628. PubMed PMC

Wilcock, D., Pisabarro, M. T., López-Hernandez, E., Serrano, L. & Coll, M. (1998). Acta Cryst. D54, 378–385. PubMed

Yamada, H., Suzuki, T., Terada, K., Takei, K., Ishikawa, K., Miwa, K., Yamashino, T. & Mizuno, T. (2001). Plant Cell Physiol.42, 1017–1023. PubMed

Najít záznam

Citační ukazatele

Nahrávání dat ...

    Možnosti archivace