1UDV
Crystal structure of the hyperthermophilic archaeal dna-binding protein Sso10b2 at 1.85 A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL17B2 |
Synchrotron site | NSRRC |
Beamline | BL17B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-06-15 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.1163 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 36.020, 134.980, 35.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 31.780 - 1.850 |
R-factor | 0.239 |
Rwork | 0.239 |
R-free | 0.27400 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 23.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.780 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.076 | 0.229 |
Number of reflections | 15639 | |
<I/σ(I)> | 15.9 | 5.8 |
Completeness [%] | 99.5 | 92.6 * |
Redundancy | 4.5 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 298 | PEG MME 550, ZnSO4, MES, pH 6.5, VAPOR DIFFUSION, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG550 MME | 25 (%) | |
3 | 1 | reservoir | 10 (mM) | ||
4 | 1 | reservoir | MES | 100 (mM) | pH6.5 |