5KQ0
Crystal structure of the A290D 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) | 0.97944 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 100.760, 113.490, 174.513 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 95.140 - 1.800 |
R-factor | 0.1535 |
Rwork | 0.152 |
R-free | 0.18480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1MWV |
RMSD bond length | 0.028 |
RMSD bond angle | 2.266 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.21) |
Refinement software | REFMAC (5.8.0151) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 95.141 | 44.523 | 1.900 |
High resolution limit [Å] | 1.800 | 5.690 | 1.800 |
Rmerge | 0.022 | 0.474 | |
Number of reflections | 181938 | ||
<I/σ(I)> | 12.3 | 24.9 | 1.6 |
Completeness [%] | 98.7 | 93.1 | 99.5 |
Redundancy | 2.9 | 3 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD |