5T63
The HhoA protease from Synechocystis sp. PCC 6803
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-22 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.9762 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 134.228, 134.228, 115.063 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 51.562 - 2.500 |
| R-factor | 0.2195 |
| Rwork | 0.217 |
| R-free | 0.26150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pv3 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.247 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | BALBES |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.880 | 51.880 | 2.600 |
| High resolution limit [Å] | 2.500 | 9.010 | 2.500 |
| Rmerge | 0.051 | 0.043 | 0.715 |
| Rmeas | 0.055 | 0.048 | 0.774 |
| Rpim | 0.021 | 0.019 | 0.293 |
| Total number of observations | 93929 | 1830 | 10766 |
| Number of reflections | 13940 | ||
| <I/σ(I)> | 20.5 | 48.1 | 2.8 |
| Completeness [%] | 100.0 | 99.3 | 100 |
| Redundancy | 6.7 | 5.6 | 6.9 |
| CC(1/2) | 0.999 | 0.998 | 0.788 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | Na-acetate pH5.0, 0.2 M MgCl2, 30% pentaerythriol propoxylate (17/8) |
