2BR1
Structure-based Design of Novel Chk1 Inhibitors: Insights into Hydrogen Bonding and Protein-Ligand Affinity
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.895, 65.714, 58.268 |
Unit cell angles | 90.00, 94.51, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
Rwork | 0.163 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ia8 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.567 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.040 | 0.230 |
Number of reflections | 21797 | |
<I/σ(I)> | 14.5 | 3.6 |
Completeness [%] | 95.1 | 95.1 |
Redundancy | 2 | 1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | pH 7.50 |