2DX6
Crystal structure of conserved hypothetical protein, TTHA0132 from Thermus thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2005-06-23 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9791, 0.9798, 0.970 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 149.967, 30.522, 62.263 |
Unit cell angles | 90.00, 110.46, 90.00 |
Refinement procedure
Resolution | 31.060 - 1.780 |
R-factor | 0.195 |
Rwork | 0.195 |
R-free | 0.23700 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.870 |
High resolution limit [Å] | 1.780 | 1.780 |
Number of reflections | 25601 | |
<I/σ(I)> | 27 | 10.57 |
Completeness [%] | 98.9 | 98.9 |
Redundancy | 3.29 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293 | 26% PEG3350, 0.1M Na Acetate, 6% iso-propanol, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |