5V53
Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei with acetate bound
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) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 100.842, 115.825, 174.775 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.230 - 1.700 |
R-factor | 0.1434 |
Rwork | 0.142 |
R-free | 0.17220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1MWV |
RMSD bond length | 0.031 |
RMSD bond angle | 2.454 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.21) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.230 | 46.230 | 1.790 |
High resolution limit [Å] | 1.700 | 5.380 | 1.700 |
Rmerge | 0.032 | 0.538 | |
Rmeas | 0.070 | 0.036 | 0.624 |
Rpim | 0.034 | 0.018 | 0.310 |
Total number of observations | 827169 | ||
Number of reflections | 214623 | ||
<I/σ(I)> | 11.7 | 19.8 | 1.4 |
Completeness [%] | 96.1 | 87.9 | 98.7 |
Redundancy | 3.9 | 3.9 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD |