9PCQ
Phosphorylation of a Conserved Aspartate at the Eukaryotic Elongation Factor 2 Kinase Catalytic Site
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-1 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-12-11 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.920099 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.464, 88.632, 154.872 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.460 - 2.300 |
| R-factor | 0.2129 |
| Rwork | 0.211 |
| R-free | 0.24290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.663 |
| Data reduction software | autoPROC |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 77.436 | 2.339 |
| High resolution limit [Å] | 2.299 | 2.299 |
| Rmeas | 0.324 | |
| Rpim | 0.088 | |
| Number of reflections | 37754 | 1877 |
| <I/σ(I)> | 6.7 | |
| Completeness [%] | 99.7 | 98.7 |
| Redundancy | 13.5 | 14.3 |
| CC(1/2) | 0.995 | 0.373 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 298.15 | Protein was mixed 1/1 with 100 mM BisTrisPropane, 80 mM NaF, 20% w/v PEG3350 |






