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 |
