1BOL
THE CRYSTAL STRUCTURE OF RIBONUCLEASE RH FROM RHIZOPUS NIVEUS AT 2.0 A RESOLUTION
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 | RIGAKU |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 67.700, 72.500, 44.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.185 |
| Rwork | 0.185 |
| Structure solution method | MIR |
| RMSD bond length | 0.016 |
| RMSD bond angle | 26.700 * |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 8.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.033 |
| Number of reflections | 11745 |
| Completeness [%] | 78.2 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.7 | 20 * | pH 6.7 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 10 (mg/ml) | |
| 2 | 1 | drop | cacodylate | 50 (mM) | |
| 3 | 1 | drop | PEG8000 | 5 (%(w/v)) | |
| 4 | 1 | reservoir | PEG8000 | 13 (%(w/v)) |
