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 |