3IVL
The Crystal Structure of the Inactive Peptidase Domain of a Putative Zinc Protease from Bordetella parapertussis to 2.2A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-14 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9794 |
Spacegroup name | H 3 |
Unit cell lengths | 108.173, 108.173, 113.995 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.330 - 2.200 |
R-factor | 0.219 |
Rwork | 0.216 |
R-free | 0.25800 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.442 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | HKL-3000 |
Refinement software | REFMAC (refmac_5.5.0102) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.180 |
High resolution limit [Å] | 2.100 | 4.520 | 2.100 |
Rmerge | 0.099 | 0.070 | 0.720 |
Number of reflections | 28929 | ||
<I/σ(I)> | 10.3 | ||
Completeness [%] | 99.6 | 96.3 | 100 |
Redundancy | 4.4 | 4.3 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 297 | 40% PEG 300, 0.1M Sodium cacodylate pH 6.5, 0.2M Calcium acetate, vapor diffusion, temperature 297K |