2D1H
Crystal structure of ST1889 protein from thermoacidophilic archaeon Sulfolobus tokodaii
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2004-03-21 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.974, 0.978432, 0.979458 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.294, 58.790, 117.476 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.370 - 2.050 |
| R-factor | 0.237 |
| Rwork | 0.237 |
| R-free | 0.27200 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.100 |
| 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] | 50.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.063 | 0.501 |
| Number of reflections | 27893 | |
| <I/σ(I)> | 31.7277 | 2.142 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 6.992 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | oil batch | 291 | oil batch, temperature 291K |
