2P5Z
The E. coli c3393 protein is a component of the type VI secretion system and exhibits structural similarity to T4 bacteriophage tail proteins gp27 and gp5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-12 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.97930 |
Spacegroup name | P 63 |
Unit cell lengths | 116.351, 116.351, 80.584 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.190 - 2.600 |
R-factor | 0.219 |
Rwork | 0.217 |
R-free | 0.26400 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.874 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.107 | 0.753 |
Number of reflections | 19128 | |
<I/σ(I)> | 6.6 | 2.8 |
Completeness [%] | 100.0 | 100 |
Redundancy | 15.5 | 15.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 0.1M Hepes pH 7.5, 21% PEG 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |