3MH7
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 ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 253.929, 253.929, 253.929 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.321 - 2.961 |
R-factor | 0.2011 |
Rwork | 0.199 |
R-free | 0.24900 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.280 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHARP |
Refinement software | PHENIX ((phenix.refine: 1.6_289)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.190 |
High resolution limit [Å] | 2.961 | 2.961 |
Rmerge | 0.093 | 0.579 |
Number of reflections | 15145 | |
<I/σ(I)> | 13 | 2.9 |
Completeness [%] | 99.7 | 99.9 |
Redundancy | 5.1 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 292 | PEG 550 MME, NaCl, pH 8.5, VAPOR DIFFUSION, temperature 292K |