1RLV
Crystal structure of a dimeric Archaeal Splicing Endonuclease
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-07-19 |
Detector | ADSC |
Wavelength(s) | 0.9795, 0.9793, 0.9998, 0.9686 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 126.817, 126.817, 130.231 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 * - 2.800* |
R-factor | 0.229 |
Rwork | 0.229 |
R-free | 0.27700 * |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.025 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 * | |
High resolution limit [Å] | 3.000 | |
Rmerge | 0.069 * | 0.189 * |
Total number of observations | 291694 * | |
Number of reflections | 21746 | |
Completeness [%] | 100.0 * | 100 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 | 298 | Pipes, KCL, ammonium sulfate, pH 6.5, EVAPORATION, 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 | PIPES | 100 (mM) | pH6.5 |
3 | 1 | reservoir | ammonium sulfate | 25-40 (mM) | |
4 | 1 | reservoir | 120-200 (mM) |