1WV8
Crystal structure of hypothetical protein TTHA1013 from an extremely thermophilic bacterium thermus thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-06-17 |
Detector | RIGAKU |
Wavelength(s) | 0.96300, 0.97911, 0.97937, 1.00000 |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 51.897, 51.897, 117.727 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 44.950 - 2.200 |
R-factor | 0.259 |
Rwork | 0.259 |
R-free | 0.27300 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.200 |
Number of reflections | 5283 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | ammonium sulfate, sodium acetate, PEG4000, Tris-HCl, Sodium chloride, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |