7CO2
HtrA-type protease AlgW 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 | 2019-06-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97891 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 95.845, 95.845, 118.765 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.180 - 2.100 |
| R-factor | 0.2353 |
| Rwork | 0.232 |
| R-free | 0.26620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1soz |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.228 |
| 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] | 39.180 | 2.173 |
| High resolution limit [Å] | 2.098 | 2.098 |
| Number of reflections | 35722 | 1891 |
| <I/σ(I)> | 24.67 | |
| Completeness [%] | 99.9 | 99.58 |
| Redundancy | 26.5 | |
| CC(1/2) | 1.000 | 0.243 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 292 | 0.2 M NACl,0.1 M Tris 8.5, 25% w/v PEG 3350 |
