1RLG
Molecular basis of Box C/D RNA-protein interaction: co-crystal structure of the Archaeal sRNP intiation complex
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 263 |
Detector technology | IMAGE PLATE |
Collection date | 2003-04-16 |
Detector | FUJI |
Wavelength(s) | 0.99, 1.09, 0.97 |
Spacegroup name | P 2 3 |
Unit cell lengths | 120.584, 120.584, 120.584 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.250 - 2.700 |
R-factor | 0.235 |
Rwork | 0.235 |
R-free | 0.26000 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 2.100 |
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] | 29.250 | 2.710 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 30750 | |
Completeness [%] | 0.9 | 54 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 7.5 | 303 | PEG 400,magnesium acetate, HEPES , pH 7.5, EVAPORATION, temperature 303K |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | PEG 400 | ||
2 | 1 | 1 | magnesium acetate | ||
3 | 1 | 1 | HEPES | ||
4 | 1 | 1 | H2O | ||
5 | 1 | 2 | PEG 400 | ||
6 | 1 | 2 | magnesium acetate | ||
7 | 1 | 2 | H2O |