5IZA
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 21 21 21 |
| Unit cell lengths | 52.465, 66.436, 82.661 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.780 - 1.500 |
| R-factor | 0.12252 |
| Rwork | 0.121 |
| R-free | 0.15921 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nmw |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.452 |
| 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] | 51.780 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.545 | 0.545 |
| Number of reflections | 46357 | |
| <I/σ(I)> | 21.27 | 2.86 |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 4.7 | 4.7 |
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 4000 |
