2EQA
Crystal Structure of the hypothetical Sua5 protein from Sulfolobus tokodaii
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 | 2006-10-07 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97915, 0.9, 0.97973 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 85.391, 120.843, 67.552 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.090 - 1.800 |
R-factor | 0.208 |
Rwork | 0.208 |
R-free | 0.23300 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
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 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.051 | 0.139 |
Number of reflections | 32701 | |
<I/σ(I)> | 52.47 | 12.1 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.9 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 0.1M Sodium Acetate, 4.0M Sodium Nitrate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |