| Literature DB >> 12136152 |
Jeong Won Nam1, Zui Fujimoto, Hiroshi Mizuno, Hisakazu Yamane, Takako Yoshida, Hiroshi Habe, Hideaki Nojiri, Toshio Omori.
Abstract
The terminal oxygenase component (CarAa) of carbazole 1,9a-dioxygenase from Pseudomonas resinovorans strain CA10 was crystallized at 293 K using the sitting-drop vapour-diffusion method under the following conditions: 0.1 M sodium citrate pH 5.6 in the presence of 0.5 M ammonium sulfate and 1.0 M lithium sulfate. By using additive reagents with the crystallizing condition, improved diffraction was obtained from the crystals. Preliminary X-ray diffraction analysis indicated that CarAa crystals are hexagonal and belong to space group P6(2) or P6(4), with unit-cell parameters a = b = 244.5, c = 65.7 A, alpha = beta = 90.0, gamma = 120.0 degrees. Diffraction data were collected to 3.0 A resolution. The V(M) value is 2.16 A(3) Da(-1), which indicates a solvent content of 43.0%. This is the first report of crystallization of the terminal oxygenase component of an angular-type dioxygenase.Entities:
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Year: 2002 PMID: 12136152 DOI: 10.1107/s0907444902009150
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449