1WWM
Crystal Structure of Conserved Hypothetical Protein TT2028 from an Extremely Thermophilic Bacterium 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 | IMAGE PLATE |
Collection date | 2004-12-20 |
Detector | RIGAKU |
Wavelength(s) | 0.96200, 0.97904, 0.97932 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.210, 101.121, 102.913 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.650 - 2.610 |
R-factor | 0.234 |
Rwork | 0.234 |
R-free | 0.27500 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.600 |
Number of reflections | 24268 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.9 | 293 | MES, PEG8000, magnesium acetate, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |