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Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase
Author(s) -
Erlandsen Heidi,
Martinez Aurora,
Knappskog Per M,
Haavik Jan,
Hough Edward,
Flatmark Torgeir
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00259-7
Subject(s) - phenylalanine hydroxylase , crystallization , phenylalanine , chemistry , crystallography , biochemistry , organic chemistry , amino acid
A recombinant truncated form (Δ1‐102/Δ428‐452) 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 Å, b =108.4 Å, c =125.7 Å. The calculated packing parameter ( V m ) is 3.24 Å 3 /Da with four 2‐fold symmetric dimers (or eight momomers) in the unit cell. Data have been collected to 2.0 Å resolution.