6MP5
Crystal structure of native human sulfide:quinone oxidoreductase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-07-10 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 119.390, 119.390, 551.858 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 90.133 - 2.990 |
| R-factor | 0.2109 |
| Rwork | 0.208 |
| R-free | 0.26420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6mo6 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.624 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.6.3) |
| Phasing software | PHASER (2.8.2) |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 96.790 | 96.790 | 3.090 |
| High resolution limit [Å] | 2.990 | 11.960 | 2.990 |
| Rmerge | 0.326 | 0.042 | 2.759 |
| Rmeas | 0.336 | 0.044 | 2.888 |
| Rpim | 0.083 | 0.013 | 0.832 |
| Total number of observations | 770154 | 11338 | 50223 |
| Number of reflections | 48607 | 953 | 4315 |
| <I/σ(I)> | 9.6 | 26.6 | 1.1 |
| Completeness [%] | 100.0 | 99.5 | 99.9 |
| Redundancy | 15.8 | 11.9 | 11.6 |
| CC(1/2) | 0.983 | 0.999 | 0.224 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 14% (w/v) PEG 4000, 10% (w/v) glycerol, 0.1M sodium acetate trihydrate pH 4.6, 0.5M ammonium acetate + 0.1% (w/v) 1,2-diheptanoyl-sn-glycero-3-phosphocholine (DHPC). Apply 1uL protein then 1uL condition (no mixing) to coverslip and seal. |
