4C51
Crystal Structure of the Catalase-Peroxidase (KatG) R418L mutant from Mycobacterium Tuberculosis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-02-20 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 150.690, 150.690, 157.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.130 - 3.100 |
R-factor | 0.16303 |
Rwork | 0.160 |
R-free | 0.21418 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cca |
RMSD bond length | 0.014 |
RMSD bond angle | 1.529 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.100 | 3.270 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.160 | 0.470 |
Number of reflections | 33364 | |
<I/σ(I)> | 11.4 | 4.5 |
Completeness [%] | 99.7 | 99.8 |
Redundancy | 7.7 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 100 MM SODIUM ACETATE, PH 4.6, 6% PEG 4000 AND 0.17 MM N-DODECYL-BETA-D-MALTOSIDE |