1V9S
Crystal structure of TT0130 protein from 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 | 2003-12-08 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 0.97874, 0.97914, 0.98400, 1.00 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 116.151, 116.151, 157.643 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.100 |
R-factor | 0.24 |
Rwork | 0.238 |
R-free | 0.27300 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
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] | 30.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.051 | 0.294 |
Number of reflections | 71836 | |
<I/σ(I)> | 15.5 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 3.3 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 5.5 | 295 | ammonium sulphate, sodium citrate, dioxane, pH 5.5, microbatch, temperature 295.0K |