4ANP
Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER |
| Temperature [K] | 90 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 66.283, 107.511, 124.550 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.280 - 2.110 |
| R-factor | 0.20467 |
| Rwork | 0.204 |
| R-free | 0.23652 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6pah |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.321 |
| Data reduction software | SAINT |
| Data scaling software | SADABS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.440 | 2.210 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.130 | 0.570 |
| Number of reflections | 25446 | |
| <I/σ(I)> | 10.84 | 2.07 |
| Completeness [%] | 97.8 | 96.2 |
| Redundancy | 6.39 | 5.77 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 40 MM PIPES, 20% PEG 2000, PH 6.8 |
