Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 5 (May 2008)


crystallization communications



Acta Cryst. (2008). F64, 402-404    [ doi:10.1107/S1744309108009123 ]

Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin

E. Alfaro, L. V. Sosa, Z. Sanoguet, B. Pastrana-Ríos and E. R. Schreiter

Abstract: Chlamydomonas reinhardtii centrin is a member of the EF-hand calcium-binding superfamily. It is found in the basal body complex and is important for flagellar motility. Like other members of the EF-hand family, centrin interacts with and modulates the function of other proteins in a calcium-dependent manner. To understand how C. reinhardtii centrin interacts with its protein targets, it has been crystallized in the presence of the model peptide melittin and X-ray diffraction data have been collected to 2.2 Å resolution. The crystals are orthorhombic, with unit-cell parameters a = 52.1, b = 114.4, c = 34.8 Å, and are likely to belong to space group P21212.

Keywords: centrin; calcium; EF-hand proteins.

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