6F5V
Crystal structure of the prephenate aminotransferase from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-10-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97967 |
| Spacegroup name | P 1 |
| Unit cell lengths | 58.470, 73.240, 103.320 |
| Unit cell angles | 92.49, 87.22, 111.05 |
Refinement procedure
| Resolution | 23.702 - 1.700 |
| R-factor | 0.1737 |
| Rwork | 0.172 |
| R-free | 0.20120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.075 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.702 | 1.740 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Number of reflections | 168766 | 11501 |
| <I/σ(I)> | 16.57 | 2.75 |
| Completeness [%] | 96.0 | 88.2 |
| Redundancy | 6.14 | 3.73 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 0.1 M Na citrate pH 4.0, 11 % PEG 4K |
