2XRI
Crystal structure of human ERI1 exoribonuclease 3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-17 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 68.720, 76.900, 86.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.490 - 2.150 |
R-factor | 0.17674 |
Rwork | 0.175 |
R-free | 0.21014 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w0h |
RMSD bond length | 0.011 |
RMSD bond angle | 1.183 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.500 | 2.300 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.110 | 0.480 |
Number of reflections | 12879 | |
<I/σ(I)> | 22.1 | 6.3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 12.6 | 13.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 0.1M TRIS PH 8.5 20% PEG MONOMETHYL ETHER 2000 0.2M TRIMETHYLAMINE N-OXIDE |