2BRN
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 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.907, 65.692, 54.429 |
Unit cell angles | 90.00, 101.81, 90.00 |
Refinement procedure
Resolution | 65.940 - 2.800 |
R-factor | 0.207 |
Rwork | 0.203 |
R-free | 0.28500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ia8 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.052 |
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 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.130 | 0.510 |
Number of reflections | 7714 | |
<I/σ(I)> | 9.1 | 1 |
Completeness [%] | 97.9 | 98.9 |
Redundancy | 3.2 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | pH 7.50 |