Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453

Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.

0.1 M bis-tris:HCl, 25% PEG 3350, 0.2 M ammonium sulfate

Phenylalanine-4-hydroxylase (E.C.1.14.16.1)

hydroxylase, phenylketonuria, PKU mutation, allostery, ACT domain, OXIDOREDUCTASE