7XS0
Trimer structure of HtrA from Helicobacter pylori bound with a tripeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-07-02 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97775 |
Spacegroup name | H 3 2 |
Unit cell lengths | 139.506, 139.506, 191.374 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.210 - 2.590 |
R-factor | 0.2322 |
Rwork | 0.231 |
R-free | 0.25820 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7xs2 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.884 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.1_4122) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.660 |
High resolution limit [Å] | 2.590 | 6.410 | 2.600 |
Rmerge | 0.064 | 0.040 | 1.634 |
Rmeas | 0.066 | 0.041 | 1.679 |
Rpim | 0.016 | 0.010 | 0.383 |
Number of reflections | 22542 | 1587 | 1460 |
<I/σ(I)> | 9.9 | ||
Completeness [%] | 100.0 | 100 | 100 |
Redundancy | 17.7 | 16.8 | 18.4 |
CC(1/2) | 0.997 | 0.848 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1 M Bis-Tris, pH 6.5, 2.2 M sodium malonate |