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- W2007883511 abstract "p-Hydroxybenzoate hydroxylase (PHBH) is an FAD-dependent monooxygenase that catalyzes the hydroxylation of p-hydroxybenzoate (pOHB) to 3,4-dihydroxybenzoate in an NADPH-dependent reaction and plays an important role in the biodegradation of aromatic compounds. PHBH from Corynebacterium glutamicum was crystallized using the hanging-drop vapour-diffusion method in the presence of NaH(2)PO(4) and K(2)HPO(4) as precipitants. X-ray diffraction data were collected to a maximum resolution of 2.5 A on a synchrotron beamline. The crystal belongs to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 94.72, c = 359.68 A, gamma = 120 degrees . The asymmetric unit contains two molecules, corresponding to a packing density of 2.65 A(3) Da(-1). The structure was solved by molecular replacement. Structure refinement is in progress." @default.
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- W2007883511 date "2007-10-24" @default.
- W2007883511 modified "2023-09-24" @default.
- W2007883511 title "Expression, purification, crystallization and initial crystallographic characterization of the<i>p</i>-hydroxybenzoate hydroxylase from<i>Corynebacterium glutamicum</i>" @default.
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- W2007883511 doi "https://doi.org/10.1107/s1744309107046386" @default.
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