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 |