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 |
