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 |