1H26
CDK2/CyclinA in complex with an 11-residue recruitment peptide from p53
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-11-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.667, 134.035, 147.936 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.880 - 2.240 |
| R-factor | 0.219 |
| Rwork | 0.216 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qmz |
| RMSD bond length | 0.017 * |
| RMSD bond angle | 1.700 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.880 | 2.360 |
| High resolution limit [Å] | 2.240 | 2.240 |
| Rmerge | 0.069 | 0.442 |
| Total number of observations | 223072 * | |
| Number of reflections | 63733 | |
| <I/σ(I)> | 9.1 | 1.3 |
| Completeness [%] | 96.5 | 75.5 |
| Redundancy | 3.3 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.4 * | 0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES PH 7.0. PROTEIN CONCENTRATION = 10MG/ML |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | pH7.4 |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | drop | EDTA | 3.4 (mM) | |
| 5 | 1 | drop | azide | 0.01 (%) | |
| 6 | 1 | drop | monothiglycerol | 0.01 (%) | |
| 7 | 1 | reservoir | 0.8 (M) | ||
| 8 | 1 | reservoir | ammonium sulfate | 1.2 (M) | |
| 9 | 1 | reservoir | HEPES | 100 (mM) | pH7.0 |
