1A25
C2 DOMAIN FROM PROTEIN KINASE C (BETA)
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 133 |
| Detector technology | CCD |
| Collection date | 1996-10 |
| Detector | PRINCETON 2K |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 77.798, 77.798, 140.826 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.700 |
| R-factor | 0.222 |
| Rwork | 0.222 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rsy |
| RMSD bond length | 0.010 |
| RMSD bond angle | 24.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.900 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.136 | 0.130 |
| Number of reflections | 12297 | |
| <I/σ(I)> | 13 | 8 |
| Completeness [%] | 98.5 | 95 |
| Redundancy | 8.9 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.4 * | 21 * | PROTEIN WAS CRYSTALLIZED FROM 15% PEG1500, 100 MM MES, PH 6.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG1500 | 15 (%(w/v)) | |
| 2 | 1 | drop | 2 (mM) | ||
| 3 | 1 | drop | o-phospho-L-serine | 2 (mM) | |
| 4 | 1 | drop | MES | 100 (mM) |
