Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin

CyaY is a 106-residue protein from Escherichia coli. It shows aminoacid seq uence similarity to human frataxin and a frataxin homologue in Saccharomyce s cerevisiae, Yfh1p. The former is associated with the disease Friedreich a taxia and the latter plays a key role in iron homeostasis in mitochondria. CyaY has been overexpressed in soluble form in E. coli. The recombinant pro tein with a His(6) tag at its C-terminus has been crystallized at 296 K usi ng polyethylene glycol (PEG) 4000 as a precipitant. Native diffraction data have been collected to 1.8 Angstrom using Cu K alpha X-rays. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell par ameters a = b = 44.66, c = 99.87 Angstrom, alpha = beta = 90.0, gamma = 120 .0 degrees. The asymmetric unit contains one molecule of recombinant CyaY, with a corresponding V-m of 2.13 Angstrom(3) Da(-1) and solvent content of 42.3%.