1CSL
CRYSTAL STRUCTURE OF THE RRE HIGH AFFINITY SITE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-05-09 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 74.500, 24.300, 46.100 |
| Unit cell angles | 90.00, 116.70, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.600 |
| R-factor | 0.211 |
| Rwork | 0.211 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 29.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.084 | 0.277 |
| Total number of observations | 30269 * | |
| Number of reflections | 9651 | |
| <I/σ(I)> | 17.6 | 3.4 |
| Completeness [%] | 96.4 | 81 |
| Redundancy | 3.1 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6 | 293 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | LI2SO4 | ||
| 2 | 1 | 1 | MGSO4 | ||
| 3 | 1 | 1 | SODIUM CACODYLATE |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 1 (mM) | |
| 2 | 1 | reservoir | 1.8 (M) | ||
| 3 | 1 | reservoir | 10 (mM) | ||
| 4 | 1 | reservoir | sodium cacodylate | 50 (mM) |
