5YFK
X-ray structure of a mutant form C232S of Clostridium perfringens sortase B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-05-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 74.670, 59.730, 56.220 |
Unit cell angles | 90.00, 121.39, 90.00 |
Refinement procedure
Resolution | 47.990 - 1.800 |
R-factor | 0.18439 |
Rwork | 0.182 |
R-free | 0.22788 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5b23 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.020 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.990 | 1.850 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.039 | 0.448 |
Number of reflections | 19621 | 5384 |
<I/σ(I)> | 20.6 | 3.2 |
Completeness [%] | 99.7 | 99.8 |
Redundancy | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 200mM ammonium phosphate monobasic, 20% (w/v) PEG 3350 |