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    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 920-921 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: CyaY is a 106-residue protein from Escherichia coli. It shows amino-acid sequence similarity to human frataxin and a frataxin homologue in Saccharomyces cerevisiae, Yfh1p. The former is associated with the disease Friedreich ataxia and the latter plays a key role in iron homeostasis in mitochondria. CyaY has been overexpressed in soluble form in E. coli. The recombinant protein with a His6 tag at its C-terminus has been crystallized at 296 K using polyethylene glycol (PEG) 4000 as a precipitant. Native diffraction data have been collected to 1.8 Å using Cu Kα X-rays. The crystals belong to the trigonal space group P3121 (or P3221), with unit-cell parameters a = b = 44.66, c = 99.87 Å, α = β = 90.0, γ = 120.0°. The asymmetric unit contains one molecule of recombinant CyaY, with a corresponding Vm of 2.13 Å3 Da−1 and solvent content of 42.3%.
    Type of Medium: Electronic Resource
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