1BDY
C2 DOMAIN FROM PROTEIN KINASE C DELTA
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 287 |
Detector technology | IMAGE PLATE |
Collection date | 1997-08 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.720, 60.690, 120.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
R-factor | 0.1976 |
Rwork | 0.198 |
R-free | 0.24730 * |
Structure solution method | MIRAS |
RMSD bond length | 0.009 |
RMSD bond angle | 1.317 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.200 |
Rmerge | 0.071 * |
Total number of observations | 36783 * |
Number of reflections | 13223 |
Completeness [%] | 96.0 |
Redundancy | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 5.6 | Pappa, H.S., (1998) Acta Cryst., D54, 693. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | PEG4000 | ||
2 | 1 | drop | protein | 5 (mg/ml) | |
3 | 1 | reservoir | PEG4000 |