5G61
S.pneumoniae ABC-transporter substrate binding protein FusA in complex with fructo-nystose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-04-23 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 76.370, 135.910, 121.190 |
| Unit cell angles | 90.00, 93.28, 90.00 |
Refinement procedure
| Resolution | 90.370 - 2.400 |
| R-factor | 0.1889 |
| Rwork | 0.186 |
| R-free | 0.25130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5g5y |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.057 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.370 | 2.460 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.210 | 0.890 |
| Number of reflections | 95973 | |
| <I/σ(I)> | 5.1 | 1.4 |
| Completeness [%] | 99.6 | 99.8 |
| Redundancy | 3.7 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | pH 8 |
