2VUX
Human ribonucleotide reductase, subunit M2 B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-04-21 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.960, 99.470, 132.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.830 - 2.800 |
R-factor | 0.213 |
Rwork | 0.209 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2uw2 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.138 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.080 | 0.660 |
Number of reflections | 22880 | |
<I/σ(I)> | 13.99 | 2.81 |
Completeness [%] | 98.1 | 99.4 |
Redundancy | 3.59 | 3.68 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.1M NACACODYLATE PH 6.5, 2.3M AMMONIUM SULFATE, 0.2M SODIUM CHLORIDE. CHYMOTRYPSIN WAS ADDED TO A RATIO CHYMOTRYPSIN:PROTEIN OF 1:100 PRIOR TO CRYSTALLISATION |