6HND
Crystal structure of the aromatic aminotransferase Aro9 from C. Albicans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-01-27 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.89429 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.377, 89.285, 161.908 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.930 - 2.230 |
| R-factor | 0.17193 |
| Rwork | 0.169 |
| R-free | 0.23024 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4je5 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.517 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.360 |
| High resolution limit [Å] | 2.230 | 2.230 |
| Rmerge | 0.154 | 0.919 |
| Number of reflections | 53903 | 8523 |
| <I/σ(I)> | 11.3 | 2.19 |
| Completeness [%] | 99.7 | 99.1 |
| Redundancy | 6 | 5.9 |
| CC(1/2) | 0.788 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.06 M MgCl2, 0.06 M CaCl2, 0.1 M Tris (base): BICINE pH 8.5, 12.5% v/v MPD, 12.5% PEG 1000, 12.5% w/v PEG 3350 |
