Abstract
CarBaBb, the class III extradiol dioxygenase involved in carbazole degradation by Pseudomonas resinovorans CA10, was crystallized at 278 K by the hanging-drop vapour-diffusion method using PEG MME 550 as a precipitant. The crystals had a transparent thin square-pillar shape and belonged to space group P21212, with unit-cell parameters a = 122.8, b = 144.6, c = 49.2 Å, α = β = γ = 90°. The crystals diffracted to a maximum resolution of 1.9 Å and gave a data set with an overall R merge of 5.7% and a completeness of 98.6%. The VM value was 2.52 Å3 Da-1, which indicated a solvent content of 51.2%.
| Original language | English |
|---|---|
| Pages (from-to) | 2340-2342 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 60 |
| Issue number | 12 II |
| DOIs | |
| Publication status | Published - 2004 Dec |
| 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 crystallographic analysis of the 2′-aminobiphenyl-2,3-diol 1,2-dioxygenase from the carbazole-degrader Pseudomonas resinovorans strain CA10. / Iwata, Kenichi; Noguchi, Haruko; Usami, Yusuke; Nam, Jeong Won; Fujimoto, Zui; Mizuno, Hiroshi; Habe, Hiroshi; Yamane, Hisakazu; Omori, Toshio; Nojiri, Hideaki.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, No. 12 II, 12.2004, p. 2340-2342.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Crystallization and preliminary crystallographic analysis of the 2′-aminobiphenyl-2,3-diol 1,2-dioxygenase from the carbazole-degrader Pseudomonas resinovorans strain CA10
AU - Iwata, Kenichi
AU - Noguchi, Haruko
AU - Usami, Yusuke
AU - Nam, Jeong Won
AU - Fujimoto, Zui
AU - Mizuno, Hiroshi
AU - Habe, Hiroshi
AU - Yamane, Hisakazu
AU - Omori, Toshio
AU - Nojiri, Hideaki
PY - 2004/12
Y1 - 2004/12
N2 - CarBaBb, the class III extradiol dioxygenase involved in carbazole degradation by Pseudomonas resinovorans CA10, was crystallized at 278 K by the hanging-drop vapour-diffusion method using PEG MME 550 as a precipitant. The crystals had a transparent thin square-pillar shape and belonged to space group P21212, with unit-cell parameters a = 122.8, b = 144.6, c = 49.2 Å, α = β = γ = 90°. The crystals diffracted to a maximum resolution of 1.9 Å and gave a data set with an overall R merge of 5.7% and a completeness of 98.6%. The VM value was 2.52 Å3 Da-1, which indicated a solvent content of 51.2%.
AB - CarBaBb, the class III extradiol dioxygenase involved in carbazole degradation by Pseudomonas resinovorans CA10, was crystallized at 278 K by the hanging-drop vapour-diffusion method using PEG MME 550 as a precipitant. The crystals had a transparent thin square-pillar shape and belonged to space group P21212, with unit-cell parameters a = 122.8, b = 144.6, c = 49.2 Å, α = β = γ = 90°. The crystals diffracted to a maximum resolution of 1.9 Å and gave a data set with an overall R merge of 5.7% and a completeness of 98.6%. The VM value was 2.52 Å3 Da-1, which indicated a solvent content of 51.2%.
UR - http://www.scopus.com/inward/record.url?scp=21644438267&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=21644438267&partnerID=8YFLogxK
U2 - 10.1107/S0907444904024485
DO - 10.1107/S0907444904024485
M3 - Article
VL - 60
SP - 2340
EP - 2342
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 12 II
ER -