1JPR
Mn substituted Ribonucleotide reductase R2 from E. coli oxidized by nitric oxide
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 | 1999-02-07 |
Detector | MARRESEARCH |
Wavelength(s) | 0.880 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.826, 84.683, 114.333 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.000 - 1.880 |
R-factor | 0.158 * |
Rwork | 0.158 |
R-free | 0.21300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Reduced wt E. coli R2 |
RMSD bond length | 0.022 |
RMSD bond angle | 1.790 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 1.950 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.069 | 0.273 |
Number of reflections | 57618 | |
Completeness [%] | 100.0 | 99.9 |
Redundancy | 4.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 20 * | Nordlund, P., (1989) FEB Lett., 258, 251. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 20 (%) | |
2 | 1 | reservoir | 0.2 (M) | ||
3 | 1 | reservoir | dioxane | 0.3 (%) | |
4 | 1 | reservoir | MES | 0.05 (M) | |
5 | 1 | drop | protein | 20 (mg/ml) |