8E9P
Crystal structure of wild-type E. coli aspartate aminotransferase 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) | 0.9795 |
| 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 | 47.080 - 2.080 |
| R-factor | 0.1774 |
| Rwork | 0.174 |
| R-free | 0.20550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1x28 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.486 |
| 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] | 62.510 | 2.130 |
| High resolution limit [Å] | 2.080 | 2.090 |
| Rmerge | 0.200 | |
| Number of reflections | 57093 | 2848 |
| <I/σ(I)> | 6.8 | |
| Completeness [%] | 100.0 | |
| Redundancy | 10.5 | |
| CC(1/2) | 0.995 | 0.227 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | HEPES, ammonium sulfate, PEG 400, maleate |
