1WNA
Crystal structure of the hypothetical protein TT1805 from Thermus thermophillus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE |
Synchrotron site | SPring-8 |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2004-05-24 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97912, 0.97944, 0.964 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 54.240, 70.691, 73.389 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.120 - 1.580 |
R-factor | 0.208 |
Rwork | 0.208 |
R-free | 0.22900 |
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 | Outer shell | |
Low resolution limit [Å] | 37.120 | 1.640 |
High resolution limit [Å] | 1.580 | 1.580 |
Number of reflections | 36267 | |
<I/σ(I)> | 17.5556 | 4.52941 |
Completeness [%] | 98.3 | 85.9 |
Redundancy | 4.61446 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 13% PEG 8000, 20% glycerol, 40mM Potassium dihydrogen phosphate, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |