7DJM
Structure of four truncated and mutated forms of quenching protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2017-12-16 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.9777 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.000, 78.750, 103.010 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.375 - 1.700 |
| R-factor | 0.187504658017 |
| Rwork | 0.186 |
| R-free | 0.21133 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7djj |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.015 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AutoSol |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmeas | 0.082 | |
| Number of reflections | 49848 | 2367 |
| <I/σ(I)> | 33.36 | |
| Completeness [%] | 99.8 | |
| Redundancy | 12.4 | |
| CC(1/2) | 0.864 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | 25-34% PEG 3350, 0.2 M NH4Ac, 0.1M MES, pH 5.9-6.6 |
