2CCA
Crystal structure of the catalase-peroxidase (KatG) and S315T mutant from Mycobacterium tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-12-17 |
| Detector | ADSC CCD |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 150.104, 150.104, 153.718 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.2 |
| Rwork | 0.199 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1MWV |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.056 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 |
| High resolution limit [Å] | 1.900 | 2.000 |
| Rmerge | 0.080 | 0.350 |
| Number of reflections | 105049 | |
| <I/σ(I)> | 26.2 | 4.6 |
| Completeness [%] | 99.0 | 96.7 |
| Redundancy | 7 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 6% PEG4000, 0.1M NA ACETATE, PH4.6, 0.17MM N-DODECYL-B-D-MALTOSIDE, PROTEIN CONCENTRATION OF 16MG/ML, pH 4.60 |
