3TD2
Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2010-06-08 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 60.310, 60.310, 87.670 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
R-factor | 0.23747 |
Rwork | 0.237 |
R-free | 0.25541 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2z2i |
RMSD bond length | 0.009 |
RMSD bond angle | 1.546 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.081 | |
Number of reflections | 6725 | |
Completeness [%] | 99.7 | |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microbatch under oil | 7.5 | 291 | 0.1M HEPES, 25% PEG 8000, 5% dioxane, pH 7.5, Microbatch under oil, temperature 291K |