6MX1
The crystal structure of the regulatory domain of aspartokinase in the bifunctional aspartokinase/homoserine dehydrogenase 1 from Escherichia coli str. K-12 substr. MG1655
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-08-13 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97934 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 92.642, 54.550, 65.242 |
| Unit cell angles | 90.00, 99.30, 90.00 |
Refinement procedure
| Resolution | 46.845 - 1.671 |
| R-factor | 0.18 |
| Rwork | 0.178 |
| R-free | 0.21550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3c1n |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.291 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.710 |
| High resolution limit [Å] | 1.670 | 1.670 |
| Rmerge | 0.072 | 0.715 |
| Rmeas | 0.084 | 0.860 |
| Rpim | 0.043 | 0.470 |
| Number of reflections | 36373 | 1678 |
| <I/σ(I)> | 26.6 | 1.48 |
| Completeness [%] | 97.9 | 91.6 |
| Redundancy | 3.5 | 2.8 |
| CC(1/2) | 0.590 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.1M Bis-Tris Propane:NaCl, 2.8 M Sodium Acetate |
