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Updated: Jun 19, 2026
Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
Published on: November 8, 2019
Expression, purification, crystallization and preliminary X-ray analysis of para-nitrophenol 4-monooxygenase from
Weidong Liu1, Wenjing Shen, Xiaoli Zhao
1Key Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural University, 210095 Nanjing, People's Republic of China.
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.
