Worrapoj OonanantJeerus SucharitakulPimchai ChaiyenJirundon YuvaniyamaMahidol UniversityChulalongkorn University2018-06-112018-06-112012-05-01Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.68, No.6 (2012), 720-723174430912-s2.0-84862164693https://repository.li.mahidol.ac.th/handle/20.500.14594/13738p-Hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) at the ortho position to yield 3,4-dihydroxyphenylacetate (DHPA). HPAH from A. baumannii is a two-component flavoprotein consisting of a smaller reductase (C 1 ) component and a larger oxygenase (C 2 ) component. The C 1 component supplies a reduced flavin in its free form to the C 2 counterpart for hydroxylation. In addition, HPA can bind to C 1 and enhance the flavin-reduction rate without becoming hydroxylated. The recombinant C 1 component was purified and crystallized using the microbatch method at 295 K. X-ray diffraction data were collected to 2.3 Å resolution using synchrotron radiation on the BL13B1 beamline at NSRRC, Taiwan. The crystal belonged to the orthorhombic space group P2 1 2 1 2 1 , with unit-cell parameters a = 47.78, b = 59.92, c = 211.85 Å, and contained two molecules of C 1 per asymmetric unit. © 2012 International Union of Crystallography All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyPhysics and AstronomyArticleSCOPUS10.1107/S1744309112016909