| Autor: |
Myong Gyong Lee, Seung-Je Cho, Jin Kuk Yang, Hyun Kyu Song, Se Won Suh |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section D (Wiley-Blackwell); Jul2000, Vol. 56 Issue 7, p920-921, 2p |
| Abstrakt: |
CyaY is a 106-residue protein from Escherichia coil. It shows amino-acid sequence similarity to human frataxin and a frataxin homologue in Saccharornyces 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. coil. 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 ų Da-1 and solvent content of 42.3%. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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