5MAI
Crystal structure of MELK in complex with an inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-10-04 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.976254 |
| Spacegroup name | I 41 3 2 |
| Unit cell lengths | 169.134, 169.134, 169.134 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 53.480 - 2.150 |
| R-factor | 0.19162 |
| Rwork | 0.189 |
| R-free | 0.23710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | in house MELK structure |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.562 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.480 | 2.270 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.063 | 0.793 |
| Number of reflections | 22725 | |
| <I/σ(I)> | 18.1 | 3.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.6 | 8.5 |
| CC(1/2) | 0.999 | 0.798 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 10-20% PEG 3350 or PEG 4000, 0.1 M BIS TRIS pH 6.5, 0.6M NaCl |
