5KQQ
Crystal structure of the W153F variant of catalase-peroxidase from B. pseudomallei treated
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-10-09 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97959 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 100.922, 116.130, 175.788 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 96.900 - 1.870 |
R-factor | 0.1451 |
Rwork | 0.143 |
R-free | 0.17520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1MWV |
RMSD bond length | 0.026 |
RMSD bond angle | 2.166 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.22) |
Refinement software | REFMAC (5.8.0151) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 96.900 | 48.448 | 1.970 |
High resolution limit [Å] | 1.870 | 5.910 | 1.870 |
Rmerge | 0.034 | 0.566 | |
Number of reflections | 153798 | ||
<I/σ(I)> | 11.1 | 16.1 | 1.3 |
Completeness [%] | 90.5 | 83.7 | 93.4 |
Redundancy | 4.7 | 4.9 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD, 0.1 M sodium citrate |