2CWQ
Crystal structure of conserved protein TTHA0727 from 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 | CCD |
Collection date | 2005-04-15 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97919, 0.97953, 0.96000 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 107.102, 107.102, 55.455 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.600 - 1.900 |
Rwork | 0.165 |
R-free | 0.21300 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
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] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 29204 | |
<I/σ(I)> | 17.54 | 8.8 |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.8 | 10.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M potassium formate, 21% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |