8FO6
Nucleotide-free structure of a functional construct of eukaryotic elongation factor 2 kinase.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-2 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-05-28 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.527, 58.901, 88.394 |
| Unit cell angles | 90.00, 109.67, 90.00 |
Refinement procedure
| Resolution | 47.520 - 2.553 |
| R-factor | 0.2176 |
| Rwork | 0.217 |
| R-free | 0.23140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7shq |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.561 |
| Data reduction software | XDS (Jan 10, 2022) |
| Data scaling software | Aimless (0.7.7) |
| Phasing software | PHASER (1.20.1_4487) |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 73.001 | 73.001 | 2.597 |
| High resolution limit [Å] | 2.553 | 6.927 | 2.553 |
| Rmerge | 0.112 | 0.048 | 0.796 |
| Rmeas | 0.123 | 0.052 | 0.875 |
| Rpim | 0.050 | 0.021 | 0.357 |
| Total number of observations | 150222 | 7797 | 7209 |
| Number of reflections | 24680 | 1300 | 1228 |
| <I/σ(I)> | 10.33 | 24.14 | 2.31 |
| Completeness [%] | 99.9 | 99.7 | 100 |
| Redundancy | 6.09 | 6 | 5.87 |
| CC(1/2) | 0.996 | 0.997 | 0.838 |
| Anomalous redundancy | 3.1 | 3.3 | 3.0 |
| CC(ano) | 0.011 | 0.112 | -0.034 |
| |DANO|/σ(DANO) | 0.8 | 0.7 | 0.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.9 | 293 | 100 mM Bis-trispropane, 200 mM NaF, 17.6% PEG-3350 (2protein 1solution) |
