5HUD
Non-covalent complex of and DAHP synthase and chorismate mutase from Corynebacterium glutamicum with bound transition state analog
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-20 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97239 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 117.622, 110.481, 134.652 |
| Unit cell angles | 90.00, 101.41, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.150 |
| R-factor | 0.25191 |
| Rwork | 0.250 |
| R-free | 0.29800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w1a |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.531 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 131.990 | 2.230 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.199 | 1.763 |
| Number of reflections | 190339 | |
| <I/σ(I)> | 4.79 | 0.44 |
| Completeness [%] | 96.7 | 85.7 |
| Redundancy | 2.95 | 2.24 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 100 mM imidazole/MES buffer, pH 6.5 30 mM each of ethylene glycol mix (di-ethylene glycol, tri-ethylene glycol, tetra-ethylene glycol, penta-ethylene glycol) 15% glycerol 15% PEG 4000 micro-seeded from badly diffracting crystals (approx. 8 AA resolution), in 100 mM Na-HEPES, pH 7.5, 200 mM LiSO4, 25% PEG 3350 |
