7OGW
Q9A mutant of Hfq protein from Neisseria meningitidis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.2 |
Synchrotron site | BESSY |
Beamline | 14.2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-10-19 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.9184 |
Spacegroup name | P 6 |
Unit cell lengths | 62.175, 62.175, 27.710 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 27.710 - 1.090 |
R-factor | 0.1017 |
Rwork | 0.101 |
R-free | 0.11760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4pno |
RMSD bond length | 0.020 |
RMSD bond angle | 2.046 |
Data reduction software | XDS (20210323) |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 31.090 | 31.090 | 1.110 |
High resolution limit [Å] | 1.090 | 5.970 | 1.090 |
Rmerge | 0.055 | 0.043 | 0.529 |
Rmeas | 0.056 | 0.044 | 0.545 |
Rpim | 0.013 | 0.010 | 0.127 |
Total number of observations | 489717 | 3286 | 22018 |
Number of reflections | 25701 | 178 | 1254 |
<I/σ(I)> | 30 | 70.4 | 5.6 |
Completeness [%] | 100.0 | 98.9 | 99.4 |
Redundancy | 19.1 | 18.5 | 17.6 |
CC(1/2) | 1.000 | 0.999 | 0.931 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | PEG3350, sodium nitrate, bis-tris propane |