8B6A
Crystal structure of BfrB protein from Bacteroides fragilis NCTC 9343
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I24 |
| Synchrotron site | Diamond |
| Beamline | I24 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-03-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.999 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 92.465, 42.311, 110.392 |
| Unit cell angles | 90.00, 95.49, 90.00 |
Refinement procedure
| Resolution | 38.470 - 1.770 |
| R-factor | 0.2082 |
| Rwork | 0.205 |
| R-free | 0.25913 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ewm |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.461 |
| Data reduction software | DIALS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.440 | 1.810 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.176 | 1.458 |
| Rpim | 0.141 | 1.078 |
| Number of reflections | 40527 | 1756 |
| <I/σ(I)> | 4.2 | 0.5 |
| Completeness [%] | 96.9 | 75.4 |
| Redundancy | 3.9 | 2.5 |
| CC(1/2) | 0.983 | 0.346 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 1.6M ammonium sulphate, 100mM sodium acetate, pH 5.5 |
