3NVT
1.95 Angstrom crystal structure of a bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase (aroA) from Listeria monocytogenes EGD-e
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 | 2010-06-30 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 111.570, 111.787, 81.049 |
| Unit cell angles | 90.00, 127.63, 90.00 |
Refinement procedure
| Resolution | 29.040 - 1.950 |
| R-factor | 0.156 |
| Rwork | 0.154 |
| R-free | 0.19800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2D8D (N-TERMINAL DOMAIN) AND 1RZM (C-TERMINAL DOMAIN) |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.254 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.097 | 0.554 |
| Number of reflections | 57343 | |
| <I/σ(I)> | 105.69 | 2.7 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 295 | Crystals grew from The Classics screen condition 68 (F8). Protein at 7.5 mg/mL in 10 mM Tris/HCl pH 8.3 0.5 M NaCl, 5 mM BME, 1 mM MnCl2, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
