6AT2
E. coli phosphoenolpyruvate carboxykinase G209N mutant bound to thiosulfate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 12.3.1 |
| Synchrotron site | ALS |
| Beamline | 12.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-12-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.1158 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 125.171, 94.360, 46.559 |
| Unit cell angles | 90.00, 96.40, 90.00 |
Refinement procedure
| Resolution | 47.180 - 1.444 |
| R-factor | 0.1716 |
| Rwork | 0.171 |
| R-free | 0.19110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2olq |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.035 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.180 | 1.520 |
| High resolution limit [Å] | 1.444 | 1.444 |
| Rmerge | 0.118 | 1.371 |
| Number of reflections | 182988 | 28555 |
| <I/σ(I)> | 7.48 | 1.04 |
| Completeness [%] | 96.3 | 92.8 |
| Redundancy | 3.8 | 3.8 |
| CC(1/2) | 0.995 | 0.530 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 24% PEG 3350, 0.4 M sodium chloride, 0.1 M Bis-Tris pH 5.5, 0.1 M sodium thiosulfate |
