5TUG
Archaellum periplasmic stator protein complex FlaF and FlaG from Sulfolobus acidocaldarius
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 12.3.1 |
| Synchrotron site | ALS |
| Beamline | 12.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9918 |
| Spacegroup name | P 61 |
| Unit cell lengths | 119.919, 119.919, 152.403 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.152 - 2.470 |
| R-factor | 0.1653 |
| Rwork | 0.163 |
| R-free | 0.19350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4p94 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.985 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless (0.5.25) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.152 | 2.560 |
| High resolution limit [Å] | 2.470 | 2.470 |
| Rmerge | 0.101 | 1.291 |
| Number of reflections | 44562 | |
| <I/σ(I)> | 19.2 | 2.4 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.4 | 11.5 |
| CC(1/2) | 0.999 | 0.774 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 288 | 18% PEG 6000 0.1M Tris, pH 7.5, 0.2M NaBr |






