Open AccessCrystallization and preliminary X‐ray characterization of full‐length Chlamydomonas reinhardtii centrin
Author(s) -
Alfaro Elisa,
Sosa Liliana del Valle,
Sanoguet Zuleika,
PastranaRíos Belinda,
Schreiter Eric R.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108009123
Subject(s) - chlamydomonas reinhardtii , orthorhombic crystal system , crystallization , crystallography , chlamydomonas , chemistry , ef hand , microbiology and biotechnology , biophysics , calcium , biology , calcium binding protein , biochemistry , mutant , crystal structure , gene , organic chemistry
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 P 2 1 2 1 2.