6CC6
Crystal structure of the W202F variant of catalase-peroxidase from B. pseudomallei
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 | 2016-07-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.467, 115.659, 174.421 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 96.390 - 1.800 |
| R-factor | 0.1513 |
| Rwork | 0.150 |
| R-free | 0.18120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MWV |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.563 |
| 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] | 96.392 | 48.196 | 1.900 |
| High resolution limit [Å] | 1.800 | 5.690 | 1.800 |
| Rmerge | 0.024 | 0.559 | |
| Rmeas | 0.076 | 0.027 | 0.627 |
| Rpim | 0.034 | 0.012 | 0.276 |
| Total number of observations | 928829 | ||
| Number of reflections | 185728 | 6108 | 27149 |
| <I/σ(I)> | 15.8 | 23.3 | 1.4 |
| Completeness [%] | 99.0 | 97.7 | 99.9 |
| Redundancy | 5 | 4.9 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | MPD, 0.1 M sodium citrate |
