2F6L
X-ray structure of Chorismate Mutase from Mycobacterium Tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-10-16 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.890, 72.930, 62.060 |
| Unit cell angles | 90.00, 103.85, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.700 |
| Rwork | 0.182 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Partially refined structure of chorismate mutase from Yersinia pestis |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.705 |
| Data reduction software | X-GEN |
| Data scaling software | X-GEN |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.000 | 1.750 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.067 | 0.380 |
| Number of reflections | 40279 | |
| <I/σ(I)> | 15.3 | 2.3 |
| Completeness [%] | 98.6 | 97.7 |
| Redundancy | 7.35 | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 303 | Reservoir solution: 0.10 M MES pH 6.5, 30% Polyethylene glycol 8K. Protein solution: 50mM Tris pH 7.5, 1mM EDTA, 1mM DTT, 200mM sodium chloride. Protein concentration was 8.3 mg/ml., VAPOR DIFFUSION, HANGING DROP, temperature 303K |
