H. Erlandsen et al., CRYSTALLIZATION AND PRELIMINARY DIFFRACTION ANALYSIS OF A TRUNCATED HOMODIMER OF HUMAN PHENYLALANINE-HYDROXYLASE, FEBS letters, 406(1-2), 1997, pp. 171-174
A recombinant truncated form (Delta 1-102/Delta 428-452) of the non-he
me 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 usi
ng the hanging drop vapour diffusion method, The crystals are orthorho
mbic, space group C222 with cell. dimensions of a=66.6 Angstrom, b=108
.4 Angstrom, c=125.7 Angstrom. The calculated packing parameter (V-m)
is 3.24 Angstrom(3)/Da with four 2-fold symmetric dimers (or eight mom
omers) in the unit cell, Data have been collected to 2.0 Angstrom reso
lution. (C) 1997 Federation of European Biochemical Societies.