4HH5
N-terminal domain (1-163) of ClpV1 ATPase from E.coli EAEC Sci1 T6SS.
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-02-03 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.931 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.860, 58.710, 65.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.770 - 2.000 |
R-factor | 0.1863 |
Rwork | 0.185 |
R-free | 0.20540 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.040 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | SHELXS |
Refinement software | BUSTER (2.11.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.049 | 0.352 |
Number of reflections | 10703 | |
<I/σ(I)> | 27.1 | 5.5 |
Completeness [%] | 96.1 | 92.1 |
Redundancy | 7.4 | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |