8P10
The crystal structure of the C-terminal domain of Mengla nucleoprotein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-05-20 |
Detector | DECTRIS EIGER2 XE 16M |
Wavelength(s) | 0.9762 |
Spacegroup name | P 1 |
Unit cell lengths | 68.309, 85.710, 146.241 |
Unit cell angles | 88.52, 76.45, 80.26 |
Refinement procedure
Resolution | 47.990 - 3.260 |
R-factor | 0.2758 |
Rwork | 0.274 |
R-free | 0.30460 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.722 |
Data reduction software | XDS |
Data scaling software | STARANISO |
Phasing software | PHASER |
Refinement software | REFMAC (V.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 142.156 | 4.052 |
High resolution limit [Å] | 3.250 | 3.256 |
Rmerge | 0.103 | 0.713 |
Number of reflections | 30881 | 6177 |
<I/σ(I)> | 8.2 | |
Completeness [%] | 89.2 | |
Redundancy | 3.7 | |
CC(1/2) | 0.998 | 0.710 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2M Ammonium sulfate, 0.1M MES pH 6.5, 30% PEG5000MME |