4AID
Crystal structure of C. crescentus PNPase bound to RNase E recognition peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-02-03 |
Detector | ADSC CCD |
Spacegroup name | H 3 |
Unit cell lengths | 157.439, 157.439, 302.379 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.600 |
R-factor | 0.21037 |
Rwork | 0.209 |
R-free | 0.25447 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gme |
RMSD bond length | 0.017 |
RMSD bond angle | 2.265 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.220 | 0.580 |
Number of reflections | 85896 | |
<I/σ(I)> | 5.5 | 2.4 |
Completeness [%] | 93.2 | 94.8 |
Redundancy | 6.3 | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 19% WT/V PEG 3350, 0.15 M DL-MALIC ACID |