5EGQ
Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-04-22 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9791 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 90.144, 96.507, 202.584 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.155 - 2.500 |
| R-factor | 0.2126 |
| Rwork | 0.211 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2phm |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.164 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.160 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.623 | |
| Number of reflections | 61203 | |
| <I/σ(I)> | 10.1 | 2 |
| Completeness [%] | 99.0 | 99.7 |
| Redundancy | 3.7 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | 0.1 M bis-tris:HCl, 25% PEG 3350, 0.2 M ammonium sulfate |
