5A0G
N-terminal thioester domain of surface protein from Clostridium perfringens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-11-29 |
| Detector | DECTRIS PILATUS |
| Spacegroup name | P 1 |
| Unit cell lengths | 70.820, 74.360, 82.810 |
| Unit cell angles | 107.32, 104.32, 98.63 |
Refinement procedure
| Resolution | 44.880 - 2.620 |
| R-factor | 0.19795 |
| Rwork | 0.196 |
| R-free | 0.22611 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.595 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.880 | 2.690 |
| High resolution limit [Å] | 2.620 | 2.620 |
| Rmerge | 0.130 | 0.760 |
| Number of reflections | 44689 | |
| <I/σ(I)> | 7.5 | 1.8 |
| Completeness [%] | 98.0 | 97.3 |
| Redundancy | 4.7 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.2 M TRI-POTASSIUM CITRATE, 20% PEG 3350 |
