5NPO
Promiscuous Protein Self-Assembly as a Function of Protein Stability
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-02-15 |
| Detector | DECTRIS EIGER R 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.909, 52.733, 67.944 |
| Unit cell angles | 90.00, 90.59, 90.00 |
Refinement procedure
| Resolution | 67.940 - 1.950 |
| R-factor | 0.20168 |
| Rwork | 0.199 |
| R-free | 0.25582 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4op5 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.913 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.940 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Number of reflections | 34416 | 1696 |
| <I/σ(I)> | 12.9 | 2.2 |
| Completeness [%] | 98.9 | 99.8 |
| Redundancy | 5.9 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 292 | 7.5% PEG 6000, 0.1M MgCl2 and 0.05M Sodium acetate pH=5.5 |
