5KSG
Crystal structure of the W153F variant of catalase-peroxidase from B. pseudomallei treated with isoniazid
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) | 0.9796 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.665, 115.928, 174.349 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 96.540 - 1.620 |
| R-factor | 0.1357 |
| Rwork | 0.135 |
| R-free | 0.15910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MWV |
| RMSD bond length | 0.032 |
| RMSD bond angle | 2.682 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | REFMAC (5.8.0151) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 96.536 | 48.358 | 1.710 |
| High resolution limit [Å] | 1.620 | 5.120 | 1.620 |
| Rmerge | 0.030 | 0.503 | |
| Rmeas | 0.069 | 0.034 | 0.563 |
| Rpim | 0.031 | 0.016 | 0.250 |
| Total number of observations | 1276157 | 41241 | 185747 |
| Number of reflections | 257891 | ||
| <I/σ(I)> | 15.1 | 37.4 | 3 |
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 4.9 | 4.8 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD, 0.1 M sodium citrate |
