6B9B
Crystal structure of the catalase-peroxidase from B. pseudomallei with maltose 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 | 2016-03-13 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.419, 115.088, 174.975 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.800 |
| R-factor | 0.137 |
| Rwork | 0.135 |
| R-free | 0.16200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MWV |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.373 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 96.153 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.568 | |
| Rmeas | 0.077 | 0.038 |
| Rpim | 0.038 | 0.019 |
| Total number of observations | 702596 | 22499 |
| Number of reflections | 184467 | 5887 |
| <I/σ(I)> | 12.9 | 33.1 |
| Completeness [%] | 98.7 | 99.8 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 20% MPD,16% PEG 4000, 0.1 M sodium citrate, 100 mM maltose |
