8E9U
Crystal structure of E. coli aspartate aminotransferase mutant HEX in the ligand-free form at 303 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] | 303 |
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 - 1.940 |
R-factor | 0.1503 |
Rwork | 0.147 |
R-free | 0.17760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x28 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.013 |
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] | 124.680 | 1.970 |
High resolution limit [Å] | 1.940 | 1.940 |
Number of reflections | 70417 | 3433 |
<I/σ(I)> | 7 | |
Completeness [%] | 99.3 | |
Redundancy | 10.2 | |
CC(1/2) | 0.997 | 0.334 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | HEPES, ammonium sulfate, PEG 400, maleate |