1OQU
A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-04-29 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.933 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.319, 91.237, 136.956 |
Unit cell angles | 90.00, 91.46, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.184 |
Rwork | 0.181 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.014 |
RMSD bond angle | 1.500 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.073 | 0.277 |
Number of reflections | 80865 | |
Completeness [%] | 98.5 | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | PEG 4000, sodium citrate, ammonium acetate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |