8HT2
Crystal structure of Acetylornithine aminotransferase from Corynebacterium glutamicum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
| Synchrotron site | PAL/PLS |
| Beamline | 7A (6B, 6C1) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2020-11-13 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 79.395, 176.766, 56.139 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.940 - 2.650 |
| R-factor | 0.2165 |
| Rwork | 0.212 |
| R-free | 0.30230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e54 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.573 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.700 |
| High resolution limit [Å] | 2.650 | 7.190 | 2.650 |
| Rmerge | 0.081 | 0.047 | 0.321 |
| Rmeas | 0.090 | 0.052 | 0.376 |
| Rpim | 0.038 | 0.022 | 0.190 |
| Total number of observations | 111467 | ||
| Number of reflections | 22995 | 1287 | 1075 |
| <I/σ(I)> | 13.3 | ||
| Completeness [%] | 97.1 | 97.6 | 92.6 |
| Redundancy | 4.8 | 5.6 | 3.3 |
| CC(1/2) | 0.997 | 0.752 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 1.6 M ammonium sulfate, 0.1 M sodium HEPES pH 6.5, 0.1 M NaCl |
