6C5C
Crystal structure of the 3-dehydroquinate synthase (DHQS) domain of Aro1 from Candida albicans SC5314 in complex with NADH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-12-05 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.678, 92.060, 88.915 |
| Unit cell angles | 90.00, 97.57, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.850 |
| R-factor | 0.17695 |
| Rwork | 0.176 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sg6 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.655 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.045 | 0.956 |
| Number of reflections | 69649 | 3533 |
| <I/σ(I)> | 37.8 | 1.44 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 4.8 | 3.5 |
| CC(1/2) | 0.717 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.2 M sodium thiocyanate, 20% PEG3350, 2 mM NADH, 0.5 mM zinc chloride, cryoprotectant: 8% glycerol, 8% ethylene glycol, 8% sucrose |
