7VO1
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 | 2021-07-02 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 1.0 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 113.740, 113.740, 290.652 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.090 - 2.990 |
R-factor | 0.2231 |
Rwork | 0.220 |
R-free | 0.28350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2eo5 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.719 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.040 |
High resolution limit [Å] | 2.990 | 8.110 | 2.990 |
Rmerge | 0.069 | 0.017 | 0.924 |
Rmeas | 0.071 | 0.018 | 0.954 |
Rpim | 0.016 | 0.004 | 0.232 |
Total number of observations | 438249 | ||
Number of reflections | 23423 | 1355 | 1114 |
<I/σ(I)> | 5.9 | ||
Completeness [%] | 100.0 | 99.4 | 99.9 |
Redundancy | 18.7 | 16.4 | 16.2 |
CC(1/2) | 1.000 | 0.906 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | PEG 3000, MgCl2, cacodylate |