@article {46433,
	title = {Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin.},
	journal = {Acta Crystallographica Section F Structural Biology and Crystallization Communications},
	volume = {64},
	year = {2008},
	month = {2008 May 1},
	pages = {402-4},
	abstract = {<p>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 A resolution. The crystals are orthorhombic, with unit-cell parameters a = 52.1, b = 114.4, c = 34.8 A, and are likely to belong to space group P2(1)2(1)2.</p>
},
	keywords = {Animals, Calcium, Calcium-Binding Proteins, Chlamydomonas reinhardtii, Crystallization, Crystallography, X-Ray, Escherichia coli, Melitten, Structure-Activity Relationship},
	issn = {1744-3091},
	doi = {10.1107/S1744309108009123},
	author = {Alfaro, Elisa and Sosa, Liliana Del Valle and Sanoguet, Zuleika and Pastrana-R{\'\i}os, Belinda and Schreiter, Eric R}
}
