3IT4
The Crystal Structure of Ornithine Acetyltransferase from Mycobacterium tuberculosis (Rv1653) at 1.7 A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.115872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.140, 99.699, 155.245 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.900 - 1.700 |
| R-factor | 0.20637 |
| Rwork | 0.204 |
| R-free | 0.24371 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vz6 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.364 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0055) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.077 | 0.321 |
| Number of reflections | 98245 | |
| <I/σ(I)> | 13.4 | 4.1 |
| Completeness [%] | 95.6 | 96.5 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Protein Concentration 13.5 mg/mL in 2.5 mM HEPES pH 7.5, precipitant 0.02 M MgCl2, 22% polyacrylic acid 5100 in 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
