4I0W
Structure of the Clostridium Perfringens CspB protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-02-15 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9794 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.876, 138.112, 140.038 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.735 - 1.600 |
R-factor | 0.1637 |
Rwork | 0.162 |
R-free | 0.18090 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 0.803 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.735 | 1.540 |
High resolution limit [Å] | 1.490 | 1.490 |
Rmerge | 0.078 | 0.451 |
Number of reflections | 202733 | |
<I/σ(I)> | 18.419 | 2.05 |
Completeness [%] | 86.8 | 46.2 |
Redundancy | 6.6 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 285.15 | 27% ethylene glycol, 50 mM sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 285.15K |