Abstract
CyaY is a 106-residue protein from Escherichia coli. It shows aminoacid 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 His 6 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 P3 121 (or P3 221), 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 V(m) of 2.13 Å 3 Da -1 and solvent content of 42.3%.
| Original language | English |
|---|---|
| Pages (from-to) | 920-921 |
| Number of pages | 2 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 56 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2000 Jul 26 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology
Cite this
Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin. / Lee, Myong Gyong; Cho, Seung Je; Yang, Jin Kuk; Song, Hyun Kyu; Suh, Se Won.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 56, No. 7, 26.07.2000, p. 920-921.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin
AU - Lee, Myong Gyong
AU - Cho, Seung Je
AU - Yang, Jin Kuk
AU - Song, Hyun Kyu
AU - Suh, Se Won
PY - 2000/7/26
Y1 - 2000/7/26
N2 - CyaY is a 106-residue protein from Escherichia coli. It shows aminoacid 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 His 6 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 P3 121 (or P3 221), 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 V(m) of 2.13 Å 3 Da -1 and solvent content of 42.3%.
AB - CyaY is a 106-residue protein from Escherichia coli. It shows aminoacid 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 His 6 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 P3 121 (or P3 221), 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 V(m) of 2.13 Å 3 Da -1 and solvent content of 42.3%.
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U2 - 10.1107/S0907444900005916
DO - 10.1107/S0907444900005916
M3 - Article
VL - 56
SP - 920
EP - 921
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 7
ER -