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 |
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ASJC Scopus subject areas
- Molecular Biology
- Biophysics
- Biochemistry
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Crystallization and Preliminary Crystallographic Analysis of Recombinant Xenopus laevis Cu, Zn Superoxide Dismutase b. / Carugo, K. D.; Collyer, C.; Coda, A.; Carri, M. T.; Battistoni, A.; Bottaro, G.; Polticelli, F.; Desideri, A.; Bolognesi, M.
In: Biochemical and Biophysical Research Communications, Vol. 194, No. 3, 16.08.1993, p. 1008-1011.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Crystallization and Preliminary Crystallographic Analysis of Recombinant Xenopus laevis Cu, Zn Superoxide Dismutase b
AU - Carugo, K. D.
AU - Collyer, C.
AU - Coda, A.
AU - Carri, M. T.
AU - Battistoni, A.
AU - Bottaro, G.
AU - Polticelli, F.
AU - Desideri, A.
AU - Bolognesi, M.
PY - 1993/8/16
Y1 - 1993/8/16
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0027279577&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027279577&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1993.1921
DO - 10.1006/bbrc.1993.1921
M3 - Article
C2 - 8352757
AN - SCOPUS:0027279577
VL - 194
SP - 1008
EP - 1011
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -