6CDQ
Crystal structure of the W202F variant of catalase-peroxidase from B. pseudomallei with INH bound.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08B1-1 |
| Synchrotron site | CLSI |
| Beamline | 08B1-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-05-30 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.531, 114.896, 174.099 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 174.099 - 1.920 |
| R-factor | 0.1676 |
| Rwork | 0.166 |
| R-free | 0.19890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDBID 1MWV |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.399 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 174.099 | 48.293 | 2.020 |
| High resolution limit [Å] | 1.920 | 6.070 | 1.920 |
| Rmerge | 0.046 | 0.516 | |
| Rmeas | 0.093 | 0.052 | 0.618 |
| Rpim | 0.048 | 0.025 | 0.331 |
| Total number of observations | 445240 | ||
| Number of reflections | 136130 | 3965 | 21573 |
| <I/σ(I)> | 9.4 | 10.6 | 1.5 |
| Completeness [%] | 88.8 | 76.5 | 97.3 |
| Redundancy | 3.3 | 3.6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD, 0.1 M sodium citrate |
