1PAH
HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424
Experimental procedure
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1996-05 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 66.600, 108.400, 125.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.176 |
Rwork | 0.176 |
R-free | 0.21800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1toh |
RMSD bond length | 0.090 |
RMSD bond angle | 25.070 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.048 | 0.390 |
Total number of observations | 18331 * | |
Number of reflections | 30932 | |
<I/σ(I)> | 20.7 | 20 |
Completeness [%] | 99.7 | 99.1 |
Redundancy | 5.9 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.8 | Erlandsen, H., (1997) FEBS Lett., 406, 171. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-12 (mg/ml) | |
2 | 1 | reservoir | PEG2000 | 12-17 (%(w/v)) | |
3 | 1 | reservoir | PIPES | 0.05-0.08 (M) |