5OL2
The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 77 |
| Detector technology | PIXEL |
| Collection date | 2015-11-17 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 177.060, 177.060, 493.150 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.866 - 3.100 |
| R-factor | 0.2113 |
| Rwork | 0.209 |
| R-free | 0.25950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4KPU and 4L1F |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.896 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.866 | 3.200 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Number of reflections | 70563 | |
| <I/σ(I)> | 11.1 | 0.9 |
| Completeness [%] | 98.9 | 98.4 |
| Redundancy | 7.2 | 7.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 0.1 M calcium acetate; 14 % (v/v) PEG 400; 0.1 M MES, pH 6.5 |
