5B6G
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 | 2015-07-01 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.448, 63.691, 52.641 |
| Unit cell angles | 90.00, 95.76, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.990 |
| R-factor | 0.1722 |
| Rwork | 0.170 |
| R-free | 0.21488 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nmw |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.514 |
| 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] | 50.000 | 2.060 |
| High resolution limit [Å] | 1.990 | 1.990 |
| Rmerge | 0.068 | 0.249 |
| Number of reflections | 23123 | |
| <I/σ(I)> | 15.16 | 5 |
| Completeness [%] | 99.2 | 99.6 |
| Redundancy | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 0.2 M Ammonium sulfate, 0.1 M Tris pH 8.0, 25 % w/v PEG 4000 |
