3SLH
1.70 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with shikimate-3-phosphate and glyphosate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97850 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.252, 186.638, 95.794 |
| Unit cell angles | 90.00, 91.51, 90.00 |
Refinement procedure
| Resolution | 29.640 - 1.700 |
| R-factor | 0.15076 |
| Rwork | 0.149 |
| R-free | 0.18169 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB code: 3ROI |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.529 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.064 | 0.480 |
| Number of reflections | 176888 | |
| <I/σ(I)> | 18.6 | 3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 295 | Protein solution: 7.5 mG/mL, 0.50 M NaCl, 0.01 M Tris-HCl (pH 8.3). Screen solution: Classics II (D7), 0.1 M Bis-Tris pH 6.5, 25% (w/v) PEG3350, VAPOR DIFFUSION, temperature 295K |
