2ZBU
Crystal structure of uncharacterized conserved protein from Thermotoga maritima
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 | 2006-12-15 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.9789, 0.9000, 0.9794 |
Spacegroup name | H 3 |
Unit cell lengths | 120.476, 120.476, 227.115 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
R-factor | 0.222 |
Rwork | 0.222 |
R-free | 0.25700 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.064 | 0.344 |
Number of reflections | 71732 | |
<I/σ(I)> | 25.8 | 4.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.5 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1M Sodium cacodylate pH6.5, 35% 2-ethoxyethanol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |