5A65
Crystal structure of mouse thiamine triphosphatase in complex with thiamine diphosphate, orthophosphate and magnesium ions.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-05-02 |
| Detector | DECTRIS PILATUS |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 105.483, 105.483, 111.805 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.390 - 1.980 |
| R-factor | 0.21027 |
| Rwork | 0.208 |
| R-free | 0.25818 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5a64 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.515 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.400 | 2.100 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.110 | 1.500 |
| Number of reflections | 44247 | |
| <I/σ(I)> | 19.66 | 1.9 |
| Completeness [%] | 99.7 | 98.6 |
| Redundancy | 25.6 | 23.85 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 27 % PEG 3350,0.2M NACL, 0.1 M TRIS PH 9.0, 0.2M MGCL2 |
