1RSV
azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide reductase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1992-09-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.893, 84.501, 113.963 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.000 - 2.200 |
| R-factor | 0.18 * |
| Rwork | 0.182 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.100 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.123 * | |
| Total number of observations | 123580 * | |
| Number of reflections | 36078 | |
| Completeness [%] | 97.3 | 97.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 20 * | Nordlund, P., (1989) FEBS Lett., 258, 251. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 20 (%) | |
| 3 | 1 | reservoir | 0.2 (M) | ||
| 4 | 1 | reservoir | dioxane | 0.3 (%) | |
| 5 | 1 | reservoir | MES | 0.05 (M) | pH6.0 |
