1B38
HUMAN CYCLIN-DEPENDENT KINASE 2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-05-21 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.333, 71.122, 72.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
Rwork | 0.180 |
R-free | 0.25000 |
Structure solution method | OTHER |
Starting model (for MR) | UNPUBLISHED |
RMSD bond length | 0.016 |
RMSD bond angle | 0.042 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.092 | 0.390 |
Total number of observations | 70729 * | |
Number of reflections | 18076 | |
<I/σ(I)> | 11 | 2.26 |
Completeness [%] | 95.2 | 96.8 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.4 | PROTEIN AT 10 MG/ML IN 10MM HEPES/HCL PH7.4, 15MM NACL WELL BUFFER CONTAINING 50MM AMMONIUM ACETATE, 12% PEG 3350, 100MM HEPES/HCL PH 7.4 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | 15 (mM) | ||
3 | 1 | drop | HEPES | 10 (mM) | |
4 | 1 | reservoir | PEG3350 | 10-15 (%) | |
5 | 1 | reservoir | ammonium acetate | 50 (mM) | |
6 | 1 | reservoir | HEPES | 0.1 (M) |