1O9K
Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID13 |
Synchrotron site | ESRF |
Beamline | ID13 |
Temperature [K] | 85 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.996, 158.548, 110.617 |
Unit cell angles | 90.00, 93.70, 90.00 |
Refinement procedure
Resolution | 50.000 * - 2.600 |
R-factor | 0.232 |
Rwork | 0.229 |
R-free | 0.28500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gux |
RMSD bond length | 0.010 |
RMSD bond angle | 1.368 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.094 * | 0.459 * |
Number of reflections | 53846 | |
<I/σ(I)> | 9.1 | |
Completeness [%] | 88.1 | |
Redundancy | 8.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.8 | 4 * | pH 7.80 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | sodium citrate | 0.14 (M) | |
3 | 1 | reservoir | PEG400 | 26 (%) | |
4 | 1 | reservoir | n-propanol | 4 (%) | |
5 | 1 | reservoir | Tris | 0.1 (M) | pH7.8 |