5KDJ
ZmpB metallopeptidase from Clostridium perfringens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-01-14 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 0.97940 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.620, 95.800, 187.220 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.820 - 2.150 |
R-factor | 0.19327 |
Rwork | 0.191 |
R-free | 0.22890 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.404 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.820 | 2.270 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.098 | 0.388 |
Number of reflections | 62638 | |
<I/σ(I)> | 13.2 | 5.3 |
Completeness [%] | 96.4 | 92.7 |
Redundancy | 6.6 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | PEG 3350, Na/K tartrate, HEPES pH 7.5 |