5KSK
Crystal structure of the catalase-peroxidase from B. pseudomallei treated with acetate
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) | 0.97949 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.703, 115.480, 174.966 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.388 - 1.690 |
| R-factor | 0.1534 |
| Rwork | 0.152 |
| R-free | 0.17960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MWV |
| RMSD bond length | 0.030 |
| RMSD bond angle | 2.396 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0151) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 115.480 | 48.388 | 1.780 |
| High resolution limit [Å] | 1.690 | 5.340 | 1.690 |
| Rmerge | 0.052 | 0.484 | |
| Rmeas | 0.081 | ||
| Rpim | 0.040 | ||
| Total number of observations | 843167 | ||
| Number of reflections | 225720 | ||
| <I/σ(I)> | 10.8 | 9.2 | 1.6 |
| Completeness [%] | 99.4 | 96.4 | 99.8 |
| Redundancy | 3.7 | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD, 0.1 M sodium citrate |
