1RSR
azide complex of the diferrous F208A 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 | 73.800, 84.200, 113.500 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.000 |
R-factor | 0.197 * |
Rwork | 0.197 |
R-free | 0.28900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 1.600 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | TNT |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.063 * | |
Total number of observations | 144767 * | |
Number of reflections | 43085 | |
Completeness [%] | 88.7 | 71.8 |
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 |