8FNY
Nucleotide-bound 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-1 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-04-06 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.9201 |
| Spacegroup name | P 1 |
| Unit cell lengths | 59.160, 83.352, 88.978 |
| Unit cell angles | 65.35, 90.03, 86.47 |
Refinement procedure
| Resolution | 37.790 - 2.220 |
| R-factor | 0.209 |
| Rwork | 0.208 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7shq |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.551 |
| Data reduction software | XDS (Jan 10, 2022) |
| Data scaling software | Aimless (0.7.7) |
| Phasing software | PHASER (1.20.1_4487) |
| Refinement software | ISOLDE (1.4) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 80.836 | 80.836 | 2.576 |
| High resolution limit [Å] | 2.220 | 7.535 | 2.222 |
| Rmerge | 0.174 | 0.082 | 0.509 |
| Rmeas | 0.205 | 0.096 | 0.596 |
| Rpim | 0.107 | 0.049 | 0.307 |
| Total number of observations | 7262 | 7183 | |
| Number of reflections | 38423 | 1920 | 1921 |
| <I/σ(I)> | 3.55 | 7.14 | 1.66 |
| Completeness [%] | 89.1 | 98.8 | 57.7 |
| Completeness (spherical) [%] | 98.8 | 7.0 | |
| Completeness (ellipsoidal) [%] | 98.8 | 57.7 | |
| Redundancy | 3.64 | 3.78 | 3.74 |
| CC(1/2) | 0.980 | 0.990 | 0.800 |
| Anomalous completeness (spherical) | 98.3 | 6.9 | |
| Anomalous completeness | 98.3 | 56.7 | |
| Anomalous redundancy | 1.9 | 1.9 | |
| CC(ano) | 0.013 | 0.058 | |
| |DANO|/σ(DANO) | 0.4 | 0.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 293 | 100 mM Bis-trispropane, 100 mM NaF, 20.5 % w/v PEG-3350 (2protein/1solution) |
