2DBS
Crystal structure of a hypothetical protein TTHC002 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 | 2005-04-16 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97924, 0.97957, 0.96000 |
Spacegroup name | P 31 |
Unit cell lengths | 41.145, 41.145, 87.572 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.000 - 2.100 |
Rwork | 0.256 |
R-free | 0.27120 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.997 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 10858 | |
<I/σ(I)> | 13.1 | 3.05 |
Completeness [%] | 96.8 | 80.7 |
Redundancy | 4.4 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.1M HEPES-Na, 1.25M Lithium Sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |