1H27
CDK2/CyclinA in complex with an 11-residue recruitment peptide from p27
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Detector technology | CCD |
Detector | ADSC CCD |
Wavelength(s) | 0.933 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.687, 133.547, 148.081 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.600 * - 2.200 |
R-factor | 0.229 |
Rwork | 0.227 |
R-free | 0.26100 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qmz |
RMSD bond length | 0.008 * |
RMSD bond angle | 1.190 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.990 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.073 | 0.399 |
Total number of observations | 181975 * | |
Number of reflections | 63569 | |
<I/σ(I)> | 6.4 | 1.4 |
Completeness [%] | 98.7 | 98.7 |
Redundancy | 2.6 | 2.6 |
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. PROTIEN 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 |