1TG2
Crystal structure of phenylalanine hydroxylase A313T mutant with 7,8-dihydrobiopterin bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-D |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-03-13 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 66.534, 107.755, 124.282 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.910 - 2.200 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.25400 |
Structure solution method | Difference fourier |
Starting model (for MR) | 1lrm |
RMSD bond length | 0.012 |
RMSD bond angle | 1.500 |
Data reduction software | d*TREK |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 22757 | |
<I/σ(I)> | 20 | 20 |
Completeness [%] | 99.0 | 99.9 |
Redundancy | 7.5 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 277 | 5-10% Ethylene Glycol, 20-40 mM Pipes, pH 6.8, 8-15% PEG 2000, VAPOR DIFFUSION, HANGING DROP, temperature 277K |