Abstract
The recombinant Cu,Zn superoxide dismutase from the South African frog Xenopus laevis, expressed in E. coli, has been crystallized in a form suitable for high resolution crystallographic investigations. The crystals grow from polyethylene glycol solutions, at pH 6.0, 28° C, and belong to the orthorhombic space group P212121 with unit cell edges a = 73.33, b = 68.86, c = 59.73 Å, one protein dimer (32,000 Mr) per asymmetric unit. Diffraction data have been collected to 3.0 Å resolution, and a molecular replacement solution found for Xenopus laevis superoxide dismutase using the bovine enzyme as search model. The crystallographic R-factor corresponding to this solution is 0.412, in the 15.0-3.0 Å resolution range.
| Original language | English |
|---|---|
| Pages (from-to) | 1008-1011 |
| Number of pages | 4 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 194 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Aug 16 1993 |
ASJC Scopus subject areas
- Molecular Biology
- Biophysics
- Biochemistry
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Cite this
Carugo, K. D., Collyer, C., Coda, A., Carri, M. T., Battistoni, A., Bottaro, G., Polticelli, F., Desideri, A., & Bolognesi, M. (1993). Crystallization and Preliminary Crystallographic Analysis of Recombinant Xenopus laevis Cu, Zn Superoxide Dismutase b. Biochemical and Biophysical Research Communications, 194(3), 1008-1011. https://doi.org/10.1006/bbrc.1993.1921