4EGR
2.50 angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with phosphoenolpyruvate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-12-19 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 162.363, 94.050, 230.510 |
| Unit cell angles | 90.00, 90.01, 90.00 |
Refinement procedure
| Resolution | 29.750 - 2.500 |
| R-factor | 0.17897 |
| Rwork | 0.177 |
| R-free | 0.22345 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3slh |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.720 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.102 | 0.567 |
| Number of reflections | 118544 | |
| <I/σ(I)> | 9.8 | 2.6 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293 | Protein: 7.5 mg/ml; 0.5 M sodium chloride, 0.01 M Tris-Hcl Screen: Pegs II F6 (Qiagen) - 0.2M Ammonium Sulfate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
