5V4O
Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei
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 | 100.828, 115.454, 175.577 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.201 - 1.950 |
R-factor | 0.1511 |
Rwork | 0.149 |
R-free | 0.18120 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1MWV |
RMSD bond length | 0.026 |
RMSD bond angle | 2.136 |
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] | 46.201 | 46.201 | 2.060 |
High resolution limit [Å] | 1.950 | 6.170 | 1.950 |
Rmerge | 0.028 | 0.438 | |
Rmeas | 0.086 | 0.033 | 0.514 |
Rpim | 0.043 | 0.017 | 0.262 |
Total number of observations | 485977 | ||
Number of reflections | 141391 | ||
<I/σ(I)> | 9.8 | 22.1 | 1.7 |
Completeness [%] | 95.0 | 88.5 | 97.3 |
Redundancy | 3.4 | 3.5 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD |