23TK
Structure of the 328-692 fragment of FlhA (A489E) form 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-07-14 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.240, 93.250, 187.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.520 - 2.900 |
| R-factor | 0.2526 |
| Rwork | 0.252 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ai0 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.689 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.200 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.107 | 0.479 |
| Number of reflections | 20281 | 3194 |
| <I/σ(I)> | 8.4 | 2.3 |
| Completeness [%] | 99.9 | |
| Redundancy | 5.1 | |
| CC(1/2) | 0.994 | 0.936 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 293 | 10% PEG3000, 0.1M KH2PO4 / Na2HPO4, 10% glycerol. Protein conc. : 10 mg/mL |






