Crystallization and preliminary X-ray analysis of AzoR (azoreductase) from Escherichia coli.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Kosuke ItoMasaru Tanokura

Abstract

AzoR (azoreductase), an FMN-dependent NADH-azo compound oxidoreductase from Escherichia coli, has been crystallized in the presence of FMN by the sitting-drop vapour-diffusion method using 2-propanol as a precipitant. AzoR catalyzes the reductive cleavage of azo groups. The crystals were found to diffract X-rays to beyond 1.8 A resolution using a synchrotron-radiation source. The crystals belonged to the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 92.2, c = 51.9 A. The crystals are expected to contain one subunit of the homodimer in the asymmetric unit (VM = 2.6 A3 Da(-1)) and to have a solvent content of 51.6%. Data sets were also collected from heavy-atom derivatives for use in phasing. As a result, crystals soaked in a solution containing K2PtCl4 for 23 d were found to be reasonably isomorphous to the native crystals and the presence of Pt atoms could be confirmed. The data sets from the native crystals and the K2PtCl4-derivatized crystals are being evaluated for use in structure determination by single isomorphous replacement with anomalous scattering.

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Citations

Feb 18, 2014·Acta Crystallographica. Section D, Biological Crystallography·Jian YuMin Yao
May 11, 2006·The Journal of Biological Chemistry·Kosuke ItoMasaru Tanokura
Feb 8, 2007·Bioscience, Biotechnology, and Biochemistry·Yoshiaki Nishiya, Yoshihiro Yamamoto
May 8, 2009·Bioscience, Biotechnology, and Biochemistry·Toshihiko OoiSeiichi Taguchi
Oct 12, 2018·Scientific Reports·Stephan EndresThomas Drepper

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