9UKR
Crystal structure of glycogen phosphorylase from E. coli in complex with AMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-01-28 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 134.915, 204.539, 263.337 |
| Unit cell angles | 90.00, 104.57, 90.00 |
Refinement procedure
| Resolution | 42.790 - 3.550 |
| R-factor | 0.226 |
| Rwork | 0.224 |
| R-free | 0.27220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.675 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.460 | 3.620 |
| High resolution limit [Å] | 3.550 | 3.550 |
| Rmerge | 0.097 | 0.861 |
| Rmeas | 0.114 | 1.031 |
| Rpim | 0.060 | 0.561 |
| Number of reflections | 83087 | 4574 |
| <I/σ(I)> | 7.1 | |
| Completeness [%] | 99.7 | 99.9 |
| Redundancy | 3.5 | 3.3 |
| CC(1/2) | 0.998 | 0.516 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | Protein conc: 10.4mg/mL; Reservoir: 0.1M MES pH 6.0, 9% (v/v) PEG 3350 |
