7B8W
Structure of LIMK1 Kinase domain with allosteric inhibitor TH-470
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I24 |
| Synchrotron site | Diamond |
| Beamline | I24 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-02-28 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9686 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.692, 83.665, 96.513 |
| Unit cell angles | 90.00, 91.97, 90.00 |
Refinement procedure
| Resolution | 50.150 - 2.800 |
| R-factor | 0.2094 |
| Rwork | 0.206 |
| R-free | 0.28620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5nxc |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.425 |
| Data reduction software | xia2 |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.200 | 51.200 | 2.940 |
| High resolution limit [Å] | 2.800 | 9.290 | 2.800 |
| Rmerge | 0.221 | 0.088 | 1.452 |
| Rmeas | 0.239 | 0.095 | 1.570 |
| Rpim | 0.091 | 0.037 | 0.595 |
| Total number of observations | 225877 | 6102 | 30054 |
| Number of reflections | 33406 | 965 | 4392 |
| <I/σ(I)> | 7 | 15.9 | 1.6 |
| Completeness [%] | 99.9 | 99.3 | 99.9 |
| Redundancy | 6.8 | 6.3 | 6.8 |
| CC(1/2) | 0.987 | 0.988 | 0.590 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 0.2M Ammonium Citrate dibasic, 20% w/v PEG 3350 |
