5XYA
Crystal structure of a serine protease from Streptococcus species
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-10-16 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.97910 |
Spacegroup name | P 62 2 2 |
Unit cell lengths | 190.530, 190.530, 248.668 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.899 - 3.000 |
R-factor | 0.2245 |
Rwork | 0.223 |
R-free | 0.27830 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5xxz |
RMSD bond length | 0.013 |
RMSD bond angle | 1.423 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (dev_2733) |
Refinement software | PHENIX ((dev_2733: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.976 |
High resolution limit [Å] | 3.000 | 2.900 |
Rmerge | 0.170 | 0.910 |
Number of reflections | 104019 | 3471 |
<I/σ(I)> | 18 | |
Completeness [%] | 98.9 | |
Redundancy | 24.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.2 M MgCl hexahydrate, 0.1 M Tris, pH 8.65, and 28% PEG3500 |