2TOH
TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT
Experimental procedure
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01 |
Detector | MARRESEARCH |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 189.464, 148.595, 56.986 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.300 |
R-factor | 0.207 |
Rwork | 0.207 |
R-free | 0.27600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1-H |
RMSD bond length | 0.020 |
RMSD bond angle | 22.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.065 | 0.310 |
Number of reflections | 17449 | |
<I/σ(I)> | 16 | 4.5 |
Completeness [%] | 95.1 | 81.6 |
Redundancy | 3.9 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 7.9 | 4 * | pH 7.9 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 16 (mg/ml) | |
2 | 1 | 2 | ammonium sulfate | 1.15 (M) | |
3 | 1 | 2 | PEG200 | 3.2 (%) | |
4 | 1 | 2 | glycerol | 5 (%) | |
5 | 1 | 2 | Tris | 100 (mM) | |
6 | 1 | 2 | 7,8-dihydrobiopterin | 3 (mM) |