7CO3
HtrA-type protease AlgWS227A with tripeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL18U1 |
Synchrotron site | SSRF |
Beamline | BL18U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2019-06-17 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97930 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 96.614, 96.614, 119.550 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.490 - 1.900 |
R-factor | 0.2362 |
Rwork | 0.234 |
R-free | 0.26950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1soz |
RMSD bond length | 0.013 |
RMSD bond angle | 1.503 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.490 | 1.996 |
High resolution limit [Å] | 1.898 | 1.898 |
Number of reflections | 49248 | 2558 |
<I/σ(I)> | 24.67 | |
Completeness [%] | 99.8 | |
Redundancy | 28.5 | |
CC(1/2) | 0.958 | 0.915 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | 0.8M Sodium/Potassium Phosphate |