2QDL
Crystal structure of scaffolding protein TtCheW from Thermoanaerobacter tengcongensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-10-17 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.214, 62.235, 55.142 |
Unit cell angles | 90.00, 115.37, 90.00 |
Refinement procedure
Resolution | 19.760 - 2.200 |
R-factor | 0.19619 |
Rwork | 0.194 |
R-free | 0.23278 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ch4 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.450 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.800 | 2.250 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.078 | 0.286 |
Number of reflections | 14589 | |
Completeness [%] | 96.0 | 93.6 |
Redundancy | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 293 | 0.1M acetate buffer (pH 5.4), 0.2M Sodium Nitrate, 10% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |