8E9S
Crystal structure of E. coli aspartate aminotransferase mutant VFCS bound to maleic acid 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) | 0.8855 |
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 | 124.490 - 2.000 |
R-factor | 0.1517 |
Rwork | 0.148 |
R-free | 0.18500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x28 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.839 |
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] | 124.490 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 64724 | 3199 |
<I/σ(I)> | 5.1 | |
Completeness [%] | 100.0 | |
Redundancy | 20 | |
CC(1/2) | 0.993 | 0.571 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | HEPES, ammonium sulfate, PEG 400, maleate |