5T69
The HhoA protease from Synechocystis sp. PCC 6803, active site mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-06-17 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97717 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 134.276, 134.276, 115.290 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 67.138 - 2.100 |
| R-factor | 0.2425 |
| Rwork | 0.241 |
| R-free | 0.27560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pv3 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.933 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.26) |
| Phasing software | BALBES |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 81.880 | 81.880 | 2.160 |
| High resolution limit [Å] | 2.100 | 8.910 | 2.100 |
| Rmerge | 0.069 | 0.068 | 0.795 |
| Rmeas | 0.072 | 0.072 | 0.830 |
| Rpim | 0.021 | 0.023 | 0.237 |
| Total number of observations | 267159 | 3416 | 22459 |
| Number of reflections | 23412 | ||
| <I/σ(I)> | 17.9 | 38.5 | 3.4 |
| Completeness [%] | 100.0 | 99.4 | 100 |
| Redundancy | 11.4 | 10 | 11.9 |
| CC(1/2) | 0.996 | 0.987 | 0.855 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | 0.1 M Na acetate pH 5.0 0.2 M Mgcl2 30% pentaerythriol propoxylate |
