5IZ9
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 | 64.133, 64.559, 84.912 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.440 - 2.930 |
| R-factor | 0.23568 |
| Rwork | 0.233 |
| R-free | 0.28234 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nmw |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.169 |
| 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] | 51.440 | 3.010 |
| High resolution limit [Å] | 2.910 | 2.910 |
| Rmerge | 0.605 | |
| Number of reflections | 7853 | |
| <I/σ(I)> | 12.45 | 3.48 |
| Completeness [%] | 99.1 | 99.9 |
| Redundancy | 4.4 | 4.6 |
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 4000 |
