4AIM
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 I24 |
Synchrotron site | Diamond |
Beamline | I24 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-14 |
Detector | MARRESEARCH MX-300 |
Spacegroup name | P 63 |
Unit cell lengths | 97.329, 97.329, 191.910 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.730 - 3.300 |
R-factor | 0.18927 |
Rwork | 0.186 |
R-free | 0.26026 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gme |
RMSD bond length | 0.011 |
RMSD bond angle | 1.703 |
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] | 40.000 | 3.480 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.140 | 0.650 |
Number of reflections | 15391 | |
<I/σ(I)> | 7.8 | 2.4 |
Completeness [%] | 99.3 | 99.2 |
Redundancy | 4.7 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 17 % WT/V PEG 3000, 0.1 M TRI-SODIUM CITRATE |