5A64
Crystal structure of mouse thiamine triphosphatase in complex with thiamine triphosphate.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-07-06 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 103.181, 93.578, 70.775 |
| Unit cell angles | 90.00, 93.04, 90.00 |
Refinement procedure
| Resolution | 70.680 - 2.100 |
| R-factor | 0.21232 |
| Rwork | 0.211 |
| R-free | 0.23199 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bhd |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.518 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.680 | 2.230 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.060 | 0.580 |
| Number of reflections | 39110 | |
| <I/σ(I)> | 19.34 | 2.36 |
| Completeness [%] | 99.5 | 98.3 |
| Redundancy | 4.58 | 4.49 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.8 | 1.6 M NA/K PHOSPHATE PH 6.8 |
