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 |
