2DSY
Crystal structure of TTHA0281 from thermus thermophilus HB8
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-01 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.97910, 0.97940, 0.98150 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.996, 62.743, 65.724 |
| Unit cell angles | 90.00, 104.31, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.185 |
| Rwork | 0.183 |
| R-free | 0.23200 |
| Structure solution method | MAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.487 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.630 | 1.970 |
| High resolution limit [Å] | 1.890 | 1.900 |
| Rmerge | 0.068 | 0.263 |
| Number of reflections | 24539 | |
| <I/σ(I)> | 16.1 | 4.66 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 9.37 | 291 | Protein 7.91mg/mL, PEG4000 17.5w/w(%), CHES-HCl 0.1M, MgCl2 0.05M, pH 9.37, Microbatch, temperature 291K |
