7TBU
Crystal structure of the 5-enolpyruvate-shikimate-3-phosphate synthase (EPSPS) domain of Aro1 from Candida albicans in complex with shikimate-3-phosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-04-25 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.987, 159.754, 55.874 |
| Unit cell angles | 90.00, 92.28, 90.00 |
Refinement procedure
| Resolution | 29.660 - 1.850 |
| R-factor | 0.1816 |
| Rwork | 0.180 |
| R-free | 0.22890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nvs |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.975 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.084 | 0.855 |
| Rpim | 0.041 | 0.589 |
| Number of reflections | 66832 | 3323 |
| <I/σ(I)> | 18.1 | 1.27 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.1 | |
| CC(1/2) | 0.502 | 0.502 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 298 | 0.4 M NaCl, 0.1 M Tris pH 8, 26%PEG3350 1mM 3-P-Shikimate cryoprotectant: 22%Et.Glycol, HEPES pH7.8 |
