6F77
Crystal structure of the prephenate aminotransferase from Rhizobium meliloti
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-11-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979310 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 103.543, 93.008, 123.069 |
| Unit cell angles | 90.00, 91.36, 90.00 |
Refinement procedure
| Resolution | 48.118 - 1.794 |
| R-factor | 0.1761 |
| Rwork | 0.174 |
| R-free | 0.20870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6f5v |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.876 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.118 | 1.900 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Number of reflections | 213629 | 33152 |
| <I/σ(I)> | 9.77 | 2.28 |
| Completeness [%] | 98.0 | 94.4 |
| Redundancy | 2.96 | 2.94 |
| CC(1/2) | 0.995 | 0.729 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 0.2 M ammonium formate, 19 % PEG 3350 |
