7VNO
Structure of aminotransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
| Synchrotron site | Photon Factory |
| Beamline | AR-NW12A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-11-30 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 113.378, 113.378, 290.041 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.990 - 1.800 |
| R-factor | 0.1745 |
| Rwork | 0.173 |
| R-free | 0.20220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2eo5 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.685 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.133 | 0.092 | 0.713 |
| Rmeas | 0.138 | 0.095 | 0.740 |
| Rpim | 0.035 | 0.023 | 0.189 |
| Total number of observations | 1426489 | ||
| Number of reflections | 102595 | 5664 | 5036 |
| <I/σ(I)> | 5.3 | ||
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 13.9 | 16.7 | 12.8 |
| CC(1/2) | 0.996 | 0.905 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | PEG 3000, MgCl2, cacodylate |
