1GEH
CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Detector | FUJI |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 233.750, 233.750, 93.260 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 100.000 - 2.800 |
| R-factor | 0.224 * |
| Rwork | 0.224 |
| R-free | 0.25400 |
| Structure solution method | SIRAS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.404 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.091 | 0.335 |
| Total number of observations | 784332 * | |
| Number of reflections | 64453 | |
| <I/σ(I)> | 11.8 | |
| Completeness [%] | 89.5 | 65.5 |
| Redundancy | 12.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 9 | 20 * | Maeda, N., (1999) J.Mol.Biol., 293, 57. * |
| 1 | Vapor diffusion, hanging drop * | 9 | 20 * | Maeda, N., (1999) J.Mol.Biol., 293, 57. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | ammonium sulfate | 1.8 (M) | |
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | drop | CHES-NaOH | 100 (mM) | pH9.0 |
