5WML
Arabidopsis thaliana Prephenate Aminotransferase mutant- K306A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2016-03-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 |
| Unit cell lengths | 51.813, 60.117, 66.734 |
| Unit cell angles | 74.78, 76.70, 83.92 |
Refinement procedure
| Resolution | 39.426 - 2.103 |
| R-factor | 0.1562 |
| Rwork | 0.153 |
| R-free | 0.21200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5wmh |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.150 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.430 | 2.140 |
| High resolution limit [Å] | 2.103 | 2.103 |
| Rmerge | 0.061 | 0.271 |
| Number of reflections | 39241 | 1947 |
| <I/σ(I)> | 11.38 | 2.02 |
| Completeness [%] | 90.0 | 86.3 |
| Redundancy | 1.8 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | 25% (w/v) PEG-1500, 100 mM MIB buffer, pH 5.0 |
