Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase.
A recombinant truncated form (delta1-102/delta428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method. The crystals are orthorhombic, space group C222 with cell dimensions of a = 66.6 A, b = 108.4 A, c = 125.7 A. The calculated packing parameter (Vm) is 3.24 A3/Da with four 2-fold symmetric dimers (or eight momomers) in the unit cell. Data have been collected to 2.0 A resolution.
Erlandsen
H
H
Department of Chemistry, Institute of Mathematical and Physical Sciences, University of Tromso, Norway.
Martinez
A
A
Knappskog
P M
PM
Haavik
J
J
Hough
E
E
Flatmark
T
T
D003460:Crystallization; D006801:Humans; D010651:Phenylalanine Hydroxylase / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D010651:Phenylalanine Hydroxylase