5A11
The crystal structure of Ta-TFP, a thiocyanate-forming protein involved in glucosinolate breakdown (space group P21)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-09-23 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.367, 89.613, 83.842 |
| Unit cell angles | 90.00, 101.08, 90.00 |
Refinement procedure
| Resolution | 45.031 - 2.470 |
| R-factor | 0.2615 |
| Rwork | 0.260 |
| R-free | 0.28760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5a10 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.078 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.030 | 2.560 |
| High resolution limit [Å] | 2.470 | 2.470 |
| Rmerge | 0.160 | 0.580 |
| Number of reflections | 24907 | |
| <I/σ(I)> | 6.94 | 2.02 |
| Completeness [%] | 98.5 | 97.5 |
| Redundancy | 3.2 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.6 | 0.1 M SODIUM CITRATE PH 5.6, 20% (W/V) PEG 3350, 0.2 M KI |
