1J3L
Structure of the RNA-processing inhibitor RraA from Thermus thermophilis
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-07-09 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 0.97900, 0.97925, 0.97000 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 61.872, 109.068, 270.319 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.500 * - 2.300 |
| R-factor | 0.21 |
| Rwork | 0.206 |
| R-free | 0.27900 * |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.500 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.084 | 0.432 |
| Number of reflections | 191090 | |
| <I/σ(I)> | 15.96 | 3.32 |
| Completeness [%] | 90.8 * | 92.3 |
| Redundancy | 5.1 * | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 * | 296 | PEG 1000, magnesium chloride, Tris-Cl, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 296K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.3 |
| 2 | 1 | reservoir | 50 (mM) | ||
| 3 | 1 | reservoir | PEG1000 | 29 (%) | |
| 4 | 1 | drop | sodium phosphate | 50 (mM) | pH7.0 |
| 5 | 1 | drop | ammonium sulfate | 1.05-0 (M) | |
| 6 | 1 | drop | Tris-HCl | 20 (mM) | |
| 7 | 1 | drop | 50 (mM) | pH8.0 | |
| 8 | 1 | drop | protein | 20.0 (mg/ml) |
