1WN9
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) | 0.979141, 0.979502, 0.964 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 74.661, 53.997, 36.201 |
Unit cell angles | 90.00, 113.93, 90.00 |
Refinement procedure
Resolution | 34.120 - 1.580 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.24600 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.500 |
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] | 34.120 | 1.640 |
High resolution limit [Å] | 1.580 | 1.580 |
Number of reflections | 34154 | |
<I/σ(I)> | 14.0589 | 7.37896 |
Completeness [%] | 99.1 | 95.6 |
Redundancy | 3.54722 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 14% PEG 8000, 0.1M NaCacodylate, 170mM ZnAcetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |