3MH6
HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-12 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 261.500, 261.500, 261.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.703 - 3.600 |
R-factor | 0.275 |
Rwork | 0.273 |
R-free | 0.30910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cs0 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.915 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.240 | 3.790 |
High resolution limit [Å] | 3.600 | 3.600 |
Rmerge | 0.243 | 0.787 |
Number of reflections | 9340 | |
<I/σ(I)> | 9.1 | 2.6 |
Completeness [%] | 99.8 | 100 |
Redundancy | 6.8 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 293 | 12% Isopropanol, 0.1M Tris, 12% PEG 2000 MME, pH 8.5, VAPOR DIFFUSION, temperature 293K |