5LI1
Structure of a Par3-inhibitory peptide bound to PKCiota core kinase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-07-04 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 82.030, 82.030, 90.790 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.010 - 2.000 |
| R-factor | 0.1537 |
| Rwork | 0.150 |
| R-free | 0.21680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3a8w |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.095 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.010 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rpim | 0.031 | 0.233 |
| Number of reflections | 25607 | |
| <I/σ(I)> | 8.3 | 1.4 |
| Completeness [%] | 99.5 | 98.6 |
| Redundancy | 5.6 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 32% Peg 2000 MME, 0.08 M KSCN |
