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Crystallization and preliminary X-ray diffraction analysis of the azoreductase PpAzoR from Pseudomonas putida MET94.

ABSTRACT: PpAzoR, an FMN-dependent NADPH azoreductase from Pseudomonas putida MET94, has been crystallized using the sitting-drop vapour-diffusion technique. The crystals diffracted to 1.6?Å resolution using synchrotron radiation and belonged to the orthorhombic space group F222, with unit-cell parameters a=72.1, b=95.5, c=146.1?Å. Data sets were collected from the native protein to 2.2?Å resolution using in-house equipment and to 1.6?Å resolution using synchrotron radiation and the three-dimensional structure was determined by the molecular-replacement method.

SUBMITTER: Correia B

PROVIDER: S-EPMC3079989 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the azoreductase PpAzoR from Pseudomonas putida MET94.

Correia Bruno B Chen Zhenjia Z Mendes Sónia S Martins Lígia O LO Bento Isabel I

Acta crystallographica. Section F, Structural biology and crystallization communications 20101223 Pt 1

PpAzoR, an FMN-dependent NADPH azoreductase from Pseudomonas putida MET94, has been crystallized using the sitting-drop vapour-diffusion technique. The crystals diffracted to 1.6 Å resolution using synchrotron radiation and belonged to the orthorhombic space group F222, with unit-cell parameters a=72.1, b=95.5, c=146.1 Å. Data sets were collected from the native protein to 2.2 Å resolution using in-house equipment and to 1.6 Å resolution using synchrotron radiation and the three-dimensional stru ...[more]

PMID: 21206041

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