3MH4
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 | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-12 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 120.708, 120.708, 232.984 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.068 - 3.100 |
R-factor | 0.2592 |
Rwork | 0.257 |
R-free | 0.30880 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ky9 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.936 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 3.210 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.092 | 0.463 |
Number of reflections | 18503 | |
<I/σ(I)> | 14.9 | 1.8 |
Completeness [%] | 97.7 | 90 |
Redundancy | 4.2 | 3.4 |
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 |