4X2D
Clostridium difficile Fic protein_0569 mutant S31A, E35A in complex with ATP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-05-15 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 158.080, 60.100, 124.830 |
| Unit cell angles | 90.00, 118.60, 90.00 |
Refinement procedure
| Resolution | 19.853 - 2.500 |
| R-factor | 0.2056 |
| Rwork | 0.205 |
| R-free | 0.23250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3cuc |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.947 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.5.5) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.990 | 2.600 | |
| High resolution limit [Å] | 2.500 | 10.000 | 2.500 |
| Rmerge | 0.076 | 0.024 | 1.442 |
| Rmeas | 0.082 | 0.026 | 1.555 |
| Total number of observations | 248377 | ||
| Number of reflections | 35941 | 597 | 3941 |
| <I/σ(I)> | 16.66 | 62.89 | 1.25 |
| Completeness [%] | 99.7 | 97.2 | 100 |
| Redundancy | 6.9 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2 M MgCl2-6xH2O, 25 % (w/v) PEG 3350, 0.1 M HEPES pH 7.5 |
