4JF1
R144Q mutant of N-acetylornithine aminotransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-07-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 97.080, 112.000, 65.320 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.750 - 1.280 |
| R-factor | 0.16821 |
| Rwork | 0.168 |
| R-free | 0.18006 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pb0 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.272 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 112.000 | 22.750 | 1.350 |
| High resolution limit [Å] | 1.280 | 4.060 | 1.280 |
| Rmerge | 0.060 | 0.020 | 0.460 |
| Number of reflections | 178148 | ||
| <I/σ(I)> | 14.1 | 39.7 | 3.2 |
| Completeness [%] | 98.3 | 99 | 95 |
| Redundancy | 4.7 | 4.9 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295 | 20% PEG 3350, 0.5M ammonium acetate, 0.1M Tris pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
