7DJL
Structure of four truncated and mutated forms of quenching protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2018-09-30 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 153.933, 166.298, 95.740 |
| Unit cell angles | 90.00, 116.82, 90.00 |
Refinement procedure
| Resolution | 44.598 - 2.961 |
| R-factor | 0.171264525779 |
| Rwork | 0.168 |
| R-free | 0.22623 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6gci |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.294 |
| 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 | 3.000 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmeas | 0.114 | |
| Number of reflections | 43808 | 2195 |
| <I/σ(I)> | 13.86 | |
| Completeness [%] | 98.3 | |
| Redundancy | 3.6 | |
| CC(1/2) | 0.780 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.3 | 287.15 | 25% PEG 3350, 0.2 M (NH4)2SO4, 0.1 M MES, pH 5.3 |
