1QMZ
PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-12-22 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 152.600, 163.700, 73.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
Rwork | 0.220 |
R-free | 0.28000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | CDK2-CYCLIN A-RECRUITMENT PEPTIDE STRUCTURE SUBMITTED ALONG WITH THIS STRUCTURE |
RMSD bond length | 0.019 |
RMSD bond angle | 0.048 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.120 | 0.510 |
Number of reflections | 51615 | |
<I/σ(I)> | 8.1 | 2.5 |
Completeness [%] | 95.4 | 95.4 |
Redundancy | 2.6 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7 | 4 * | pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-15 (mg/ml) | |
2 | 1 | drop | peptide | 1 (mM) | |
3 | 1 | drop | AMPPNP | 1 (mM) |