1. Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase
- Author
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Jan Haavik, Edward Hough, Heidi Erlandsen, Aurora Martinez, Torgeir Flatmark, and Per M. Knappskog
- Subjects
Diffraction ,Phenylalanine hydroxylase ,Stereochemistry ,Polythylene glycol ,Biophysics ,Phenylalanine ,Biochemistry ,law.invention ,X-ray diffraction analysis ,Maltose-binding protein ,X-Ray Diffraction ,Structural Biology ,law ,Genetics ,Humans ,Crystallization ,Molecular Biology ,biology ,Chemistry ,Phenylalanine Hydroxylase ,Cell Biology ,Recombinant Proteins ,Recombinant enzyme ,biology.protein ,Recombinant DNA ,Orthorhombic crystal system ,Truncated form - Abstract
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.
- Published
- 1997