Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase

H Erlandsen; A Martinez; P M Knappskog; J Haavik; E Hough; T Flatmark

doi:10.1016/s0014-5793(97)00259-7

Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase

FEBS Lett. 1997 Apr 7;406(1-2):171-4. doi: 10.1016/s0014-5793(97)00259-7.

Authors

H Erlandsen¹, A Martinez, P M Knappskog, J Haavik, E Hough, T Flatmark

Affiliation

¹ Department of Chemistry, Institute of Mathematical and Physical Sciences, University of Tromso, Norway.

PMID: 9109411
DOI: 10.1016/s0014-5793(97)00259-7

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Humans
Phenylalanine Hydroxylase / chemistry*
Recombinant Proteins / chemistry
X-Ray Diffraction

Substances

Recombinant Proteins
Phenylalanine Hydroxylase