4IWB
Novel Fold of FliC/FliS Fusion Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 61.129, 66.157, 97.169 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.090 - 1.750 |
| R-factor | 0.21008 |
| Rwork | 0.209 |
| R-free | 0.23235 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.883 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.790 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.073 | 0.441 |
| Number of reflections | 39366 | |
| <I/σ(I)> | 19.7 | |
| Completeness [%] | 96.8 | 88.2 |
| Redundancy | 5.9 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 290 | 38% PEG500 MME, 0.1 M sodium chloride, 0.1 M Tris-HCl, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
