8HT4
Crystal structure of Acetylornithine aminotransferase complex with PLP 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 | 2021-04-07 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 109.284, 119.023, 55.017 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.510 - 2.510 |
| R-factor | 0.175 |
| Rwork | 0.171 |
| R-free | 0.25420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 8ht2 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.633 |
| 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 | 2.540 |
| High resolution limit [Å] | 2.500 | 6.780 | 2.500 |
| Rmerge | 0.153 | 0.148 | 0.283 |
| Rmeas | 0.166 | 0.163 | 0.308 |
| Rpim | 0.064 | 0.065 | 0.118 |
| Total number of observations | 161300 | ||
| Number of reflections | 24581 | 1367 | 1192 |
| <I/σ(I)> | 11.7 | ||
| Completeness [%] | 97.2 | 97.6 | 97.5 |
| Redundancy | 6.6 | 5.9 | 6.6 |
| CC(1/2) | 0.972 | 0.932 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 12% (W/V) PEG 3350, 8% Tacsimate pH 5.0 |
