8E9J
Crystal structure of E. coli aspartate aminotransferase mutant HEX in the ligand-free form at 278 K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 278 |
Detector technology | PIXEL |
Collection date | 2021-06-01 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.1158 |
Spacegroup name | P 63 |
Unit cell lengths | 143.830, 143.830, 81.570 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 124.560 - 2.090 |
R-factor | 0.1705 |
Rwork | 0.168 |
R-free | 0.19750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x28 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.494 |
Data reduction software | xia2 |
Data scaling software | DIALS |
Phasing software | PHASER |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 124.700 | 2.130 |
High resolution limit [Å] | 2.090 | 2.090 |
Rmerge | 0.315 | |
Number of reflections | 56805 | 2782 |
<I/σ(I)> | 5.9 | |
Completeness [%] | 99.8 | |
Redundancy | 10.2 | |
CC(1/2) | 0.993 | 0.273 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | HEPES, ammonium sulfate, PEG 400, maleate |