2BRB
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 | 44.993, 65.770, 58.360 |
Unit cell angles | 90.00, 94.29, 90.00 |
Refinement procedure
Resolution | 57.740 - 2.100 |
R-factor | 0.243 |
Rwork | 0.241 |
R-free | 0.27200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ia8 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.990 |
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 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.080 | 0.440 |
Number of reflections | 20050 | |
<I/σ(I)> | 13 | 2.7 |
Completeness [%] | 96.6 | 83.2 |
Redundancy | 4 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | pH 7.50 |