Crystallization and preliminary X-ray studies of methyl parathion hydrolase from Pseudomonas sp. WBC-3

Authors: Sun, Lei; Dong, Yanjie; Zhou, Yafeng; Yang, Maojun; Zhang, Chenggang; Rao, Zihe; Zhang, Xian-en

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 954-956(3)

Publisher: Blackwell Publishing

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Abstract:

Methyl parathion hydrolase (MPH) from Pseudomonas sp. WBC-3, an enzyme that catalyzes the degradation of methyl parathion (O,O-dimethyl O-p-nitrophenyl phosphorothioate; MP), has been purified and crystallized by the hanging-drop vapour-diffusion method. The crystals were grown at 291 K using a precipitant solution consisting of 30% PEG 400, 0.1 M sodium acetate pH 4.6, 0.1 M CdCl₂. MPH is a zinc-containing enzyme judged by inductively coupled plasma mass-spectrometric (ICP-MS) analysis. Multiple-wavelength anomalous dispersive X-ray data were collected at 2.5 Å resolution from a single crystal on beamline 41XU at SPring-8. The crystal belongs to space group P4₃2₁2, with unit-cell parameters a = 84.94, b = 84.94, c = 200.38 Å, α = β = γ = 90°. The asymmetric unit contains two molecules and has a solvent content of ∼52%. Crystal structure determination is in progress.

Keywords: methyl parathion hydrolase; organophosphate pesticides; biodegradation

Document Type: Research article

DOI: 10.1107/S0907444904005669

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