3TI2
1.90 Angstrom resolution crystal structure of N-terminal domain 3-phosphoshikimate 1-carboxyvinyltransferase from Vibrio cholerae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-22 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.758, 40.072, 133.861 |
| Unit cell angles | 90.00, 90.33, 90.00 |
Refinement procedure
| Resolution | 29.810 - 1.900 |
| R-factor | 0.1534 |
| Rwork | 0.151 |
| R-free | 0.19557 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nvs |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.943 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.097 | 0.569 |
| Number of reflections | 65572 | |
| <I/σ(I)> | 13.8 | 2.6 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | Protein: 4.0 mGr/mL, 0.25 M Sodium chloride, 0.01 M Tris-HCl (pH 8.3) Crystallization: Classics II (Qiagen) condition D10 0.1 M Bis-Tris pH 6.5 20% (w/v) PEG 5000 MME, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
