2WEV
Truncation and Optimisation of Peptide Inhibitors of CDK2, Cyclin A Through Structure Guided Design
Replaces: 2C5PExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 74.523, 113.844, 158.462 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.300 |
R-factor | 0.18992 |
Rwork | 0.187 |
R-free | 0.24270 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ol1 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.354 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.420 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.090 | 0.280 |
Number of reflections | 60655 | |
<I/σ(I)> | 15.7 | |
Completeness [%] | 96.4 | 80.4 |
Redundancy | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.8 | PEG3350 30% V/V, 0.1M TRI-SODIUM CITRATE, pH 7.8 |