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

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Acta Crystallographica Section F Structural Biology and Crystallization Communications. 2008 May 1;64(Pt 5):402-4. doi: 10.1107/S1744309108009123

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

Alfaro E, Sosa LD, Sanoguet Z, Pastrana-Ríos B, Schreiter ER

Note: Research in this publication was not performed at Janelia.

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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 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.

PMID: 18453711 [PubMed - indexed for MEDLINE]

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

Note: Research in this publication was not performed at Janelia.

Abstract

PMID: 18453711 [PubMed - indexed for MEDLINE]

Janelia Authors