7T88
Crystal Structure of the C-terminal Domain of the Phosphate Acetyltransferase from Escherichia coli
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 | 2021-12-04 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 72.875, 72.875, 193.248 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.260 - 2.100 |
| R-factor | 0.2013 |
| Rwork | 0.200 |
| R-free | 0.23090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | alpha Fold2 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.534 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.19_4092) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.159 | 1.642 |
| Number of reflections | 31287 | 1515 |
| <I/σ(I)> | 24.1 | 1.19 |
| Completeness [%] | 100.0 | 99 |
| Redundancy | 14 | 7.9 |
| CC(1/2) | 0.973 | 0.535 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.2 M Ammonium Sulfate, 0.1 M Bis-Tris:HCl pH 6.5, 25% (w/v) PEG 3350 |
