5KDN
ZmpB metallopeptidase from Clostridium perfringens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08B1-1 |
Synchrotron site | CLSI |
Beamline | 08B1-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-05-28 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.97950 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.890, 68.020, 170.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.090 - 1.660 |
R-factor | 0.15508 |
Rwork | 0.154 |
R-free | 0.18046 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5kdj |
RMSD bond length | 0.018 |
RMSD bond angle | 1.863 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.090 | 1.680 |
High resolution limit [Å] | 1.660 | 1.660 |
Rmerge | 0.054 | 0.249 |
Number of reflections | 92133 | |
<I/σ(I)> | 18.5 | 5.3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.2 | 6.6 |
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 |