1WS6
The Structure of Thermus thermphillus HB8 hypothetical protein TTHA0928
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL12B2 |
Synchrotron site | SPring-8 |
Beamline | BL12B2 |
Temperature [K] | 174 |
Detector technology | CCD |
Collection date | 2003-02-18 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.88, 0.9795, 0.9795, 1.03 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 58.760, 58.760, 101.660 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
R-factor | 0.222 |
Rwork | 0.218 |
R-free | 0.28300 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.274 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.077 | 0.335 |
Number of reflections | 7434 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.7 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.5 | 278 | PEG 10000, potassium thiocyanate, pH 6.5, micro-batch, temperature 278K |