8CRC
Structure of human Plk1 PBD in complex with Allopole-A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-06-10 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.999 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.359, 51.905, 51.446 |
Unit cell angles | 90.00, 106.64, 90.00 |
Refinement procedure
Resolution | 37.710 - 1.650 |
R-factor | 0.1791 |
Rwork | 0.177 |
R-free | 0.21860 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.351 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.290 | 1.680 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.068 | 0.881 |
Rmeas | 0.080 | 1.034 |
Rpim | 0.042 | 0.536 |
Number of reflections | 23444 | 1144 |
<I/σ(I)> | 9.7 | 2 |
Completeness [%] | 97.6 | 96.4 |
Redundancy | 7 | 7.1 |
CC(1/2) | 0.999 | 0.883 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 295 | 12% (w/v) PEG 3350, 0.1 M MES |