5W1D
Crystal Structure of Mouse Protocadherin-15 EC4-7
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-10 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97910 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 78.863, 78.863, 289.469 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 76.090 - 3.350 |
| R-factor | 0.22955 |
| Rwork | 0.227 |
| R-free | 0.27884 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5t4m 5tpk |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.620 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.090 | 3.410 |
| High resolution limit [Å] | 3.350 | 3.350 |
| Rmerge | 0.134 | 0.601 |
| Number of reflections | 14064 | 596 |
| <I/σ(I)> | 16.9 | 2.5 |
| Completeness [%] | 98.5 | 86.4 |
| Redundancy | 11.2 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 0.1 M Tris pH 8.5 2.0 M MgAc 23% PEG 400 |
