5KT8
Crystal structure of the W139F variant of the 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) | 0.9795 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.651, 112.782, 174.539 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.356 - 2.000 |
| R-factor | 0.152 |
| Rwork | 0.150 |
| R-free | 0.18630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MWV |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.041 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | REFMAC (5.8.0151) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 174.539 | 48.356 | 2.110 |
| High resolution limit [Å] | 2.000 | 6.320 | 2.000 |
| Rmerge | 0.020 | 0.546 | |
| Rmeas | 0.090 | 0.023 | 0.627 |
| Rpim | 0.042 | 0.011 | 0.300 |
| Total number of observations | 505864 | 16153 | 73044 |
| Number of reflections | 126470 | ||
| <I/σ(I)> | 14.6 | 54.9 | 2.4 |
| Completeness [%] | 94.5 | 88.8 | 96.5 |
| Redundancy | 4 | 4 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD, 0.1 M sodium citrate, isoniazid |
