9ZQG
Crystal structure of B. burgdorferi HtrA protease domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X17B1 |
| Synchrotron site | NSLS |
| Beamline | X17B1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-06-23 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.92010 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 114.877, 114.877, 102.533 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.160 - 2.000 |
| R-factor | 0.1915 |
| Rwork | 0.189 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.939 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.160 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.022 | 0.700 |
| Number of reflections | 17834 | 1757 |
| <I/σ(I)> | 13.3 | 0.9 |
| Completeness [%] | 99.9 | 99.6 |
| Redundancy | 2 | |
| CC(1/2) | 0.999 | 0.531 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 2 M sodium chloride and 10% Polyethylene glycol 6000 |
