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 |