6CFQ
Crystal structure of the D141N variant of catalase-peroxidase from B. pseudomallei with INH 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 | 2016-07-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.641, 115.506, 174.546 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 96.320 - 1.720 |
| R-factor | 0.1429 |
| Rwork | 0.141 |
| R-free | 0.17040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDBID 1MWV |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.497 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 96.325 | 48.148 | 1.810 |
| High resolution limit [Å] | 1.720 | 5.440 | 1.720 |
| Rmerge | 0.021 | 0.575 | |
| Rmeas | 0.061 | 0.023 | 0.642 |
| Rpim | 0.027 | 0.010 | 0.282 |
| Total number of observations | 1075073 | ||
| Number of reflections | 215015 | 7245 | 31100 |
| <I/σ(I)> | 19.9 | 27.2 | 1.4 |
| Completeness [%] | 99.9 | 99.8 | 99.8 |
| Redundancy | 5 | 4.8 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 20% MPD, 0.1 M sodium citrate, 17% PEG 4000 |
