4GS4
Structure of the alpha-tubulin acetyltransferase, alpha-TAT1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-05-01 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 2 2 2 |
| Unit cell lengths | 97.931, 130.668, 37.423 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.797 - 2.112 |
| R-factor | 0.2294 |
| Rwork | 0.227 |
| R-free | 0.25320 |
| Structure solution method | SAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.282 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 39.800 |
| High resolution limit [Å] | 2.100 |
| Number of reflections | 26218 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298.5 | 0.1M Tris pH 7.5, 2.7M Sodium Formate, VAPOR DIFFUSION, HANGING DROP, temperature 298.5K |






