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- W2017130247 abstract "Para-nitrophenol 4-monooxygenase (PnpA) plays an important role in bacterial degradation of para-nitrophenol by oxidative release of the nitro group from the aromatic ring to form p-benzoquinone. In order to understand the structural basis of the function of this enzyme, PnpA was cloned, expressed in Escherichia coli and purified. PnpA was crystallized by the hanging-drop vapour-diffusion technique with PEG 4000 as precipitant. The PnpA crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.47, b = 77.56, c = 209.17 A, and diffracted to 2.24 A resolution." @default.
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- W2017130247 date "2009-09-23" @default.
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- W2017130247 title "Expression, purification, crystallization and preliminary X-ray analysis ofpara-nitrophenol 4-monooxygenase fromPseudomonas putidaDLL-E4" @default.
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- W2017130247 doi "https://doi.org/10.1107/s1744309109032370" @default.
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