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 |
