7VNT
Structure of aminotransferase-substrate complex
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 | 113.747, 113.747, 289.562 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.300 - 1.920 |
| R-factor | 0.1827 |
| Rwork | 0.181 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2eo5 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.653 |
| 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 | 1.950 |
| High resolution limit [Å] | 1.920 | 5.210 | 1.920 |
| Rmerge | 0.126 | 0.065 | 1.163 |
| Rmeas | 0.129 | 0.067 | 1.196 |
| Rpim | 0.029 | 0.016 | 0.276 |
| Total number of observations | 1640839 | ||
| Number of reflections | 84821 | 4682 | 4147 |
| <I/σ(I)> | 4 | ||
| Completeness [%] | 99.5 | 99.1 | 99 |
| Redundancy | 19.3 | 17.8 | 18.4 |
| CC(1/2) | 0.998 | 0.861 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | PEG 3000, MgCl2, cacodylate |
