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 |






