5LIH
Structure of a peptide-substrate bound to PKCiota core kinase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-04-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 78.980, 84.230, 111.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 67.280 - 3.250 |
| R-factor | 0.258 |
| Rwork | 0.257 |
| R-free | 0.28360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3a8w |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.733 |
| Data reduction software | xia2 |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.280 | 3.430 |
| High resolution limit [Å] | 3.250 | 3.250 |
| Rmerge | 0.172 | 0.475 |
| Number of reflections | 12144 | |
| <I/σ(I)> | 6.3 | 2.5 |
| Completeness [%] | 99.6 | 99.9 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 32% Peg 2000 MME, 0.08 M KSCN |
