8JOQ
Plk1 polo-box domain bound to HPV18 L2 residues 209-215 with pThr213
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 5C (4A) |
Synchrotron site | PAL/PLS |
Beamline | 5C (4A) |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2023-03-09 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.987 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 35.143, 54.346, 57.295 |
Unit cell angles | 90.00, 90.61, 90.00 |
Refinement procedure
Resolution | 35.141 - 1.796 |
R-factor | 0.21 |
Rwork | 0.206 |
R-free | 0.24970 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.891 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.830 |
High resolution limit [Å] | 1.796 | 1.800 |
Number of reflections | 18536 | 958 |
<I/σ(I)> | 5.5 | |
Completeness [%] | 91.8 | |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.1M malate MES Tris buffer pH 6.5, 25% polyethylene glycol 1500 |