7WWO
Dimer form of hypothetical protein TTHA1873 from Thermus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-12 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0723 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 90.422, 90.422, 141.707 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 68.630 - 2.170 |
| R-factor | 0.1874 |
| Rwork | 0.186 |
| R-free | 0.21710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7wrk |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.590 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.630 | 2.240 |
| High resolution limit [Å] | 2.170 | 2.170 |
| Number of reflections | 18800 | 1575 |
| <I/σ(I)> | 5.6 | |
| Completeness [%] | 99.9 | |
| Redundancy | 9.9 | |
| CC(1/2) | 0.959 | 0.906 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 277 | 60% v/v Tacsimate pH 7.0 |
