8GM4
Functional construct of the Eukaryotic elongation factor 2 kinase bound to an ATP-competitive inhibitor
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 | 80.544, 60.684, 88.704 |
| Unit cell angles | 90.00, 111.10, 90.00 |
Refinement procedure
| Resolution | 47.730 - 2.120 |
| R-factor | 0.2086 |
| Rwork | 0.207 |
| R-free | 0.23760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7shq |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.515 |
| Data reduction software | XDS (Jan 10, 2022 (BUILT 20220220)) |
| 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] | 75.133 | 75.133 | 2.044 |
| High resolution limit [Å] | 2.009 | 5.452 | 2.009 |
| Rmerge | 0.207 | 0.084 | 3.651 |
| Rmeas | 0.227 | 0.092 | 3.985 |
| Rpim | 0.092 | 0.038 | 1.583 |
| Total number of observations | 320683 | 16913 | 16164 |
| Number of reflections | 53518 | 2786 | 2638 |
| <I/σ(I)> | 4.97 | 13.32 | 0.68 |
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 5.99 | 6.07 | 6.13 |
| CC(1/2) | 0.985 | 0.978 | 0.311 |
| Anomalous redundancy | 3.1 | 3.2 | 3.1 |
| CC(ano) | -0.096 | -0.089 | -0.009 |
| |DANO|/σ(DANO) | 0.7 | 0.6 | 0.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.2 | 295.15 | Cocktail:16.55% PEG-3350, 200 mM NaF, 100 mM BisTris-Propane Protein sol: 10.3 mg/mL 20 mM Tris pH 7.5, 100 mM NaCl, 3 mM CaCl2, 1mM TCEP, 0.3 mM ADP, 0.3 m Inhibitor , 0.7 % DMSO 2protein/1cocktail (0.2 ul total) |
