5IZ6
Protein-protein interaction
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2015-06-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.396, 63.215, 52.768 |
| Unit cell angles | 90.00, 95.61, 90.00 |
Refinement procedure
| Resolution | 52.570 - 2.150 |
| R-factor | 0.16515 |
| Rwork | 0.163 |
| R-free | 0.20609 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nmw |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.363 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.570 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.196 | |
| Number of reflections | 18356 | |
| <I/σ(I)> | 11.17 | 2.04 |
| Completeness [%] | 99.4 | |
| Redundancy | 3 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 0.2M Ammonium sulfate 0.1M Tris pH 8.0, 25% w/v PEG 3350 |
