6XSX
The structure of the catalytic module of the metalloprotease ZmpA from Clostridium perfringens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-05-10 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97530 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.168, 54.553, 90.984 |
Unit cell angles | 90.00, 93.20, 90.00 |
Refinement procedure
Resolution | 30.780 - 2.100 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.22770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5kdn |
RMSD bond length | 0.004 |
RMSD bond angle | 1.105 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.212 | 0.960 |
Rpim | 0.084 | 0.386 |
Number of reflections | 34596 | 1700 |
<I/σ(I)> | 9.7 | 2.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.4 | 7.2 |
CC(1/2) | 0.963 | 0.734 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 0.1 M MES:NaOH and 12% PEG 20000 |