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

Journal Article · · Acta Crystallographica. Section F
 [1]; ;  [1];  [1]
  1. Chemistry Department, University of Puerto Rico, Mayagüez (Puerto Rico)

C. reinhardtii centrin, an EF-hand calcium-binding protein localized to the microtubule-organizing center of eukaryotic organisms, has been crystallized in the presence of the model peptide melittin. X-ray diffraction data were collected to 2.2 Å resolution. 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 P2{sub 1}2{sub 1}2.

OSTI ID:
22360564
Journal Information:
Acta Crystallographica. Section F, Vol. 64, Issue Pt 5; Other Information: PMCID: PMC2376399; PMID: 18453711; PUBLISHER-ID: en5296; OAI: oai:pubmedcentral.nih.gov:2376399; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English